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1
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0036089390
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Conformational regulation of integrin structure and function
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A thorough and provocative review of conformational change in integrins, particularly in I domains, and how it regulates affinity for ligand.
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Shimaoka M., Takagi J., Springer T.A. Conformational regulation of integrin structure and function. Annu Rev Biophys Biomol Struct. 31:2002;485-516. A thorough and provocative review of conformational change in integrins, particularly in I domains, and how it regulates affinity for ligand.
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Annu Rev Biophys Biomol Struct
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, pp. 485-516
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Shimaoka, M.1
Takagi, J.2
Springer, T.A.3
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2
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0037145037
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Integrins: Bi-directional, allosteric, signalling machines
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An excellent recent overview on integrins.
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Hynes R.O. Integrins: bi-directional, allosteric, signalling machines. Cell. 110:2002;673-687. An excellent recent overview on integrins.
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Cell
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Hynes, R.O.1
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3
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0023661323
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CDNA cloning and complete primary structure of the α subunit of a leukocyte adhesion glycoprotein, p150,95
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Corbi A.L., Miller L.J., O'Connor K., Larson R.S., Springer T.A. cDNA cloning and complete primary structure of the α subunit of a leukocyte adhesion glycoprotein, p150,95. EMBO J. 6:1987;4023-4028.
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EMBO J
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Corbi, A.L.1
Miller, L.J.2
O'Connor, K.3
Larson, R.S.4
Springer, T.A.5
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4
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0024004133
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Amino acid sequence of the murine Mac-1 alpha chain reveals homology with the integrin family and an additional domain related to von Willebrand factor
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Pytela R. Amino acid sequence of the murine Mac-1 alpha chain reveals homology with the integrin family and an additional domain related to von Willebrand factor. EMBO J. 7:1988;1371-1378.
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EMBO J
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, pp. 1371-1378
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Pytela, R.1
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5
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0028986196
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Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18)
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Lee J.-O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18). Cell. 80:1995;631-638.
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Cell
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Lee, J.-O.1
Rieu, P.2
Arnaout, M.A.3
Liddington, R.4
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6
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0028959231
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The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted β-sheet flanked by α-helices found in human ras-p21
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Edwards Y.J.K., Perkins S.J. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted β-sheet flanked by α-helices found in human ras-p21. FEBS Lett. 358:1995;283-286.
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FEBS Lett
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Edwards, Y.J.K.1
Perkins, S.J.2
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8
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0030990436
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Folding of the conserved domain but not of flanking regions in the integrin β2 subunit requires association with the α subunit
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Huang C., Lu C., Springer T.A. Folding of the conserved domain but not of flanking regions in the integrin β2 subunit requires association with the α subunit. Proc Natl Acad Sci USA. 94:1997;3156-3161.
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Proc Natl Acad Sci USA
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, pp. 3156-3161
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Huang, C.1
Lu, C.2
Springer, T.A.3
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9
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0031029272
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A structure prediction for the ligand-binding region of the integrin β subunit: Evidence for the presence of a von Willebrand factor A domain
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Tuckwell D.S., Humphries M.J. A structure prediction for the ligand-binding region of the integrin β subunit: evidence for the presence of a von Willebrand factor A domain. FEBS Lett. 400:1997;297-303.
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FEBS Lett
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Tuckwell, D.S.1
Humphries, M.J.2
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10
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0022448122
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Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin
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Tamkun J.W., DeSimone D.W., Fonda D., Patel R.S., Buck C., Horwitz A.F., Hynes R.O. Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell. 46:1986;271-282.
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Cell
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Tamkun, J.W.1
DeSimone, D.W.2
Fonda, D.3
Patel, R.S.4
Buck, C.5
Horwitz, A.F.6
Hynes, R.O.7
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11
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0023666090
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Cloning of the β subunit of the leukocyte adhesion proteins: Homology to an extracellular matrix receptor defines a novel supergene family
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Kishimoto T.K., O'Connor K., Lee A., Roberts T.M., Springer T.A. Cloning of the β subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family. Cell. 48:1987;681-690.
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Cell
, vol.48
, pp. 681-690
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Kishimoto, T.K.1
O'Connor, K.2
Lee, A.3
Roberts, T.M.4
Springer, T.A.5
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12
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0035949665
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Definition of EGF-like, closely interacting modules that bear activation epitopes in integrin β subunits
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Prediction of integrin EGF-like domains and their disulfide bond connectivity.
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Takagi J., Beglova N., Yalamanchili P., Blacklow S.C., Springer T.A. Definition of EGF-like, closely interacting modules that bear activation epitopes in integrin β subunits. Proc Natl Acad Sci USA. 98:2001;11175-11180. Prediction of integrin EGF-like domains and their disulfide bond connectivity.
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Proc Natl Acad Sci USA
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, pp. 11175-11180
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Takagi, J.1
Beglova, N.2
Yalamanchili, P.3
Blacklow, S.C.4
Springer, T.A.5
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13
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0023582252
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Amino acid sequence of the human fibronectin receptor
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Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D., Ruoslahti E. Amino acid sequence of the human fibronectin receptor. J Cell Biol. 105:1987;1183-1190.
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J Cell Biol
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Argraves, W.S.1
Suzuki, S.2
Arai, H.3
Thompson, K.4
Pierschbacher, M.D.5
Ruoslahti, E.6
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14
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0023664558
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Structure of the platelet membrane glycoprotein IIb: Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors
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Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., Schwartz E., Bennett J.S. Structure of the platelet membrane glycoprotein IIb: homology to the alpha subunits of the vitronectin and fibronectin membrane receptors. J Biol Chem. 262:1987;8476-8482.
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J Biol Chem
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Poncz, M.1
Eisman, R.2
Heidenreich, R.3
Silver, S.M.4
Vilaire, G.5
Surrey, S.6
Schwartz, E.7
Bennett, J.S.8
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15
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0031013031
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Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain
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Springer T.A. Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proc Natl Acad Sci USA. 94:1997;65-72.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 65-72
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Springer, T.A.1
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16
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0035850669
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Crystal structure of the extracellular segment of integrin αVβ3
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The important determination of the crystal structure of integrin αVβ3.
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Xiong J.-P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., Joachimiak A., Goodman S.L., Arnaout M.A. Crystal structure of the extracellular segment of integrin αVβ3. Science. 294:2001;339-345. The important determination of the crystal structure of integrin αVβ3.
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Science
, vol.294
, pp. 339-345
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Xiong, J.-P.1
Stehle, T.2
Diefenbach, B.3
Zhang, R.4
Dunker, R.5
Scott, D.L.6
Joachimiak, A.7
Goodman, S.L.8
Arnaout, M.A.9
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17
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0036220127
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Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
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Based on a prediction, integrin EGF-like domains were expressed in E. coli, refolded and used for NMR structure determination. The structure localizes integrin activation epitopes to buried positions in the bent αVβ3 structure, suggesting that it represents the low affinity conformation.
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Beglova N., Blacklow S.C., Takagi J., Springer T.A. Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat Struct Biol. 9:2002;282-287. Based on a prediction, integrin EGF-like domains were expressed in E. coli, refolded and used for NMR structure determination. The structure localizes integrin activation epitopes to buried positions in the bent αVβ3 structure, suggesting that it represents the low affinity conformation.
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(2002)
Nat Struct Biol
, vol.9
, pp. 282-287
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Beglova, N.1
Blacklow, S.C.2
Takagi, J.3
Springer, T.A.4
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18
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0001290687
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Domains in plexins: Links to integrins and transcription factors
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Bork P., Doerks T., Springer T.A., Snel B. Domains in plexins: links to integrins and transcription factors. Trends Biochem Sci. 24:1999;261-263.
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(1999)
Trends Biochem Sci
, vol.24
, pp. 261-263
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Bork, P.1
Doerks, T.2
Springer, T.A.3
Snel, B.4
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19
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0032491379
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An extracellular β-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components
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Springer T.A. An extracellular β-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components. J Mol Biol. 283:1998;837-862.
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(1998)
J Mol Biol
, vol.283
, pp. 837-862
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Springer, T.A.1
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20
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0035013711
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Implications for familial hypercholesterolemia from structure of the LDL receptor YWTD-EGF domain pair
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The β-propeller prediction was used to guide the expression of a fragment containing the β-propeller domain and flanking EGF-like domains. The 1.5 Å structure yields important insights into the YWTD β-propeller fold and the molecular basis for a large number of LDLR mutations.
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Jeon H., Meng W., Takagi J., Eck M.J., Springer T.A., Blacklow S.C. Implications for familial hypercholesterolemia from structure of the LDL receptor YWTD-EGF domain pair. Nat Struct Biol. 8:2001;499-504. The β-propeller prediction was used to guide the expression of a fragment containing the β-propeller domain and flanking EGF-like domains. The 1.5 Å structure yields important insights into the YWTD β-propeller fold and the molecular basis for a large number of LDLR mutations.
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(2001)
Nat Struct Biol
, vol.8
, pp. 499-504
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Jeon, H.1
Meng, W.2
Takagi, J.3
Eck, M.J.4
Springer, T.A.5
Blacklow, S.C.6
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21
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0036796740
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Essay from the genome annotation series: Distribution and evolution of the von Willebrand/integrin A domain: A widely dispersed domain with roles in cell adhesion and elsewhere
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An excellent review of VWA domains from a phylogenetic perspective, with reference to integrin I and I-like domains.
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Whittaker C.A., Hynes R.O. Essay from the genome annotation series: distribution and evolution of the von Willebrand/integrin A domain: a widely dispersed domain with roles in cell adhesion and elsewhere. Mol Biol Cell. 13:2002;3369-3387. An excellent review of VWA domains from a phylogenetic perspective, with reference to integrin I and I-like domains.
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(2002)
Mol Biol Cell
, vol.13
, pp. 3369-3387
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Whittaker, C.A.1
Hynes, R.O.2
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22
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0030581168
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Assessment of protein fold predictions from sequence information: The predicted α/β doubly wound fold of the von Willebrand factor type A domain is similar to its crystal structure
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Edwards Y.J.K., Perkins S.J. Assessment of protein fold predictions from sequence information: the predicted α/β doubly wound fold of the von Willebrand factor type A domain is similar to its crystal structure. J Mol Biol. 260:1996;277-285.
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J Mol Biol
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, pp. 277-285
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Edwards, Y.J.K.1
Perkins, S.J.2
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23
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0027483226
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A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding
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Michishita M., Videm V., Arnaout M.A. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 72:1993;857-867.
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Cell
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Michishita, M.1
Videm, V.2
Arnaout, M.A.3
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24
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0029889988
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PHD: Predicting one-dimensional protein structure by profile based neural networks
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Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266:1996;525-539.
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Methods Enzymol
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, pp. 525-539
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Rost, B.1
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25
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0034647506
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Structural and functional studies with antibodies to the integrin β2 subunit: A model for the I-like domain
-
Out of twelve secondary structure elements shared by I and I-like domains, seven were aligned perfectly. Whereas adjusting the sequence alignment to the template using packing quality scores worked well for highly constrained β-propeller domains, it did not work well for this α/β fold. Although all five incorrectly aligned secondary structure elements were only misaligned by 1 to 3 residues, in each case the alignment would have been improved by centering the predicted secondary structure on the template secondary structure.
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Huang C., Zang Q., Takagi J., Springer T.A. Structural and functional studies with antibodies to the integrin β2 subunit: a model for the I-like domain. J Biol Chem. 275:2000;21514-21524. Out of twelve secondary structure elements shared by I and I-like domains, seven were aligned perfectly. Whereas adjusting the sequence alignment to the template using packing quality scores worked well for highly constrained β-propeller domains, it did not work well for this α/β fold. Although all five incorrectly aligned secondary structure elements were only misaligned by 1 to 3 residues, in each case the alignment would have been improved by centering the predicted secondary structure on the template secondary structure.
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(2000)
J Biol Chem
, vol.275
, pp. 21514-21524
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Huang, C.1
Zang, Q.2
Takagi, J.3
Springer, T.A.4
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26
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0033910699
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Evolution of domain families
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A phylogenetic distribution of domain families. The integrin I-like domain is shown to be a VWA family member using PSI-BLAST.
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Ponting C.P., Schultz J., Copley R.R., Andrade M.A., Bork P. Evolution of domain families. Adv Protein Chem. 54:2000;185-244. A phylogenetic distribution of domain families. The integrin I-like domain is shown to be a VWA family member using PSI-BLAST.
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Adv Protein Chem
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, pp. 185-244
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Ponting, C.P.1
Schultz, J.2
Copley, R.R.3
Andrade, M.A.4
Bork, P.5
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27
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0032568655
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SMART, a simple modular architecture research tool: Identification of signaling domains
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Schultz J., Milpetz F., Bork P., Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA. 95:1998;5857-5864.
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Schultz, J.1
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Ponting, C.P.4
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28
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0035748996
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Comparison of performance in successive CASP experiments
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A supplement in Proteins analyzes the results and is the place to find out how well these techniques work. For fold recognition, automatic structure prediction is currently no match for computation augmented by expert human knowledge and is being separately evaluated in Critical Assessment of Fully Automated Structure Prediction (CAFASP).
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Venclovas C, Zemla A, Fidelis K, Moult J. Comparison of performance in successive CASP experiments, Proteins Suppl 2001:163-170. Every two years, the latest prediction techniques are tested at CASP ( http://PredictionCenter.llnl.gov/ ). A supplement in Proteins analyzes the results and is the place to find out how well these techniques work. For fold recognition, automatic structure prediction is currently no match for computation augmented by expert human knowledge and is being separately evaluated in Critical Assessment of Fully Automated Structure Prediction (CAFASP).
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Proteins Suppl
, pp. 163-170
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Venclovas, C.1
Zemla, A.2
Fidelis, K.3
Moult, J.4
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29
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0025145061
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Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: Homology of integrin cysteine-rich repeats to domain III of laminin B chains
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Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D. Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: homology of integrin cysteine-rich repeats to domain III of laminin B chains. Int Immunol. 2:1990;1097-1108.
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Int Immunol
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Yuan, Q.1
Jiang, W.-M.2
Krissansen, G.W.3
Watson, J.D.4
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30
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0033106290
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Cloning and characterization of a novel β integrin-related cDNA coding for the protein TIED ("ten β integrin EGF-like repeat domains") that maps to chromosome band 13q33: A divergent stand-alone integrin stalk structure
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Berg R.W., Leung E., Gough S., Morris C., Yao W.-P., Wang S., Ni J., Krissansen G.W. Cloning and characterization of a novel β integrin-related cDNA coding for the protein TIED ("ten β integrin EGF-like repeat domains") that maps to chromosome band 13q33: a divergent stand-alone integrin stalk structure. Genomics. 56:1999;169-178.
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Genomics
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Berg, R.W.1
Leung, E.2
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Morris, C.4
Yao, W.-P.5
Wang, S.6
Ni, J.7
Krissansen, G.W.8
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31
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0035823114
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Defining the repeating elements in the cysteine-rich region (CRR) of the CD18 integrin β2 subunit
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Excellent experimental work defining the boundaries of integrin EGF-like domains.
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Tan S.-M., Walters S.E., Mathew E.C., Robinson M.K., Drbal K., Shaw J.M., Law S.K. Defining the repeating elements in the cysteine-rich region (CRR) of the CD18 integrin β2 subunit. FEBS Lett. 505:2001;27-30. Excellent experimental work defining the boundaries of integrin EGF-like domains.
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FEBS Lett
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, pp. 27-30
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Tan, S.-M.1
Walters, S.E.2
Mathew, E.C.3
Robinson, M.K.4
Drbal, K.5
Shaw, J.M.6
Law, S.K.7
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32
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0032540845
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Homology-based fold predictions for Mycoplasma genitalium proteins
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Huynen M., Doerks T., Eisenhaber F., Orengo C., Sunyaev S., Yuan Y., Bork P. Homology-based fold predictions for Mycoplasma genitalium proteins. J Mol Biol. 280:1998;323-326.
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J Mol Biol
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Huynen, M.1
Doerks, T.2
Eisenhaber, F.3
Orengo, C.4
Sunyaev, S.5
Yuan, Y.6
Bork, P.7
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33
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0028054340
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A secondary structure model of the integrin α subunit N-terminal domain based on analysis of multiple alignments
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Tuckwell D.S., Humphries M.J., Brass A. A secondary structure model of the integrin α subunit N-terminal domain based on analysis of multiple alignments. Cell Adhes Commun. 2:1994;385-402.
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Cell Adhes Commun
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Tuckwell, D.S.1
Humphries, M.J.2
Brass, A.3
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34
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Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing
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Jones D.T., Miller R.T., Thornton J.M. Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing. Proteins. 23:1995;387-397.
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Jones, D.T.1
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35
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0026671355
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Structural principles for the propeller assembly of β-sheets: The preference for seven-fold symmetry
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Murzin A.G. Structural principles for the propeller assembly of β-sheets: the preference for seven-fold symmetry. Proteins. 14:1992;191-201.
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Proteins
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Murzin, A.G.1
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WHAT IF: A molecular modeling and drug design program
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Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph. 8:1990;52-56.
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J Mol Graph
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Vriend, G.1
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37
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0033858742
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Integrin structure
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An excellent review of structural knowledge about integrins and their ligand-binding sites before the αVβ3 crystal structure was determined.
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Humphries M.J. Integrin structure. Biochem Soc Trans. 28:2000;311-339. An excellent review of structural knowledge about integrins and their ligand-binding sites before the αVβ3 crystal structure was determined.
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Biochem Soc Trans
, vol.28
, pp. 311-339
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Humphries, M.J.1
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38
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0035941265
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Amino acid residues in the αIIb subunit that are critical for ligand binding to integrin αIIbβ3 are clustered in the β-propeller model
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Mutagenesis combined with the β-propeller model goes a long way toward defining the ligand-binding site on integrin αIIbβ3.
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Kamata T., Tieu K.K., Springer T.A., Takada Y. Amino acid residues in the αIIb subunit that are critical for ligand binding to integrin αIIbβ3 are clustered in the β-propeller model. J Biol Chem. 276:2001;44275-44283. Mutagenesis combined with the β-propeller model goes a long way toward defining the ligand-binding site on integrin αIIbβ3.
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(2001)
J Biol Chem
, vol.276
, pp. 44275-44283
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Kamata, T.1
Tieu, K.K.2
Springer, T.A.3
Takada, Y.4
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39
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0037023363
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Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
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Xiong J.P., Stehle T., Zhang R., Joachimiak A., Frech M., Goodman S.L., Arnaout M.A. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science. 295:2002;151-155.
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Science
, vol.295
, pp. 151-155
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Xiong, J.P.1
Stehle, T.2
Zhang, R.3
Joachimiak, A.4
Frech, M.5
Goodman, S.L.6
Arnaout, M.A.7
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40
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0032475963
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Supersites within superfolds. Binding site similarity in the absence of homology
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Russell R.B., Sasieni P.D., Sternberg M.J. Supersites within superfolds. Binding site similarity in the absence of homology. J Mol Biol. 282:1998;903-918.
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Russell, R.B.1
Sasieni, P.D.2
Sternberg, M.J.3
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41
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0032544737
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The cation-binding domain from the α subunit of integrin α5β1 is a minimal domain for fibronectin recognition
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Baneres J.L., Roquet F., Green M., LeCalvez H., Parello J. The cation-binding domain from the α subunit of integrin α5β1 is a minimal domain for fibronectin recognition. J Biol Chem. 273:1998;24744-24753.
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J Biol Chem
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Baneres, J.L.1
Roquet, F.2
Green, M.3
LeCalvez, H.4
Parello, J.5
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43
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0032574691
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Experimental support for a β-propeller domain in integrin α-subunits and a calcium binding site on its lower surface
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Oxvig C., Springer T.A. Experimental support for a β-propeller domain in integrin α-subunits and a calcium binding site on its lower surface. Proc Natl Acad Sci USA. 95:1998;4870-4875.
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Proc Natl Acad Sci USA
, vol.95
, pp. 4870-4875
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Oxvig, C.1
Springer, T.A.2
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44
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0027292152
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Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
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2+-binding β-hairpin loop better resembles integrin sequence motifs than the EF-hand
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Structure and distribution of modules in extracellular proteins
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Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
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Crennell S., Garman E., Laver G., Vimr E., Taylor G. Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure. 2:1994;535-544.
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Archaeal surface layer proteins contain β-propeller, polycystic kidney disease, and β-helix domains, and are related to metazoan cell surface proteins
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A combined prediction and crystal structure study.
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Jing H., Takagi J., Liu J., Lindgren S., Zhang R.-G., Joachimiak A., Wang J., Springer T.A. Archaeal surface layer proteins contain β-propeller, polycystic kidney disease, and β-helix domains, and are related to metazoan cell surface proteins. Structure. 10:2002;1453-1464. A combined prediction and crystal structure study.
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49
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Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation
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Lu C., Ferzly M., Takagi J., Springer T.A. Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation. J Immunol. 166:2001;5629-5637.
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Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
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EM image reconstruction demonstrates interconversion between one bent and two extended integrin conformations. Mutagenic introduction of a disulfide bond to stabilize the bent conformation abolishes activation of cell surface integrins.
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Takagi J., Petre B.M., Walz T., Springer T.A. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell. 110:2002;599-611. EM image reconstruction demonstrates interconversion between one bent and two extended integrin conformations. Mutagenic introduction of a disulfide bond to stabilize the bent conformation abolishes activation of cell surface integrins.
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51
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IIbβ3 "inside-out" activation as regulated by its cytoplasmic face
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A unique orientation between integrin α and β subunit cytoplasmic domains is found that is consistent with previous mutagenesis studies.
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IIbβ3 "inside-out" activation as regulated by its cytoplasmic face. Cell. 110:2002;587-597. A unique orientation between integrin α and β subunit cytoplasmic domains is found that is consistent with previous mutagenesis studies.
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52
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Association of the membrane-proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state
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Lu C., Takagi J., Springer T.A. Association of the membrane-proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state. J Biol Chem. 276:2001;14642-14648.
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C-terminal opening mimics "inside-out" activation of integrin α5β1
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Takagi J., Erickson H.P., Springer T.A. C-terminal opening mimics "inside-out" activation of integrin α5β1. Nat Struct Biol. 8:2001;412-416.
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54
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Computational design of an integrin I domain stabilized in the open, high affinity conformation
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Repacking the hydrophobic core of the αM integrin I domain to stabilize the open, high affinity conformation, or the closed, low affinity conformation.
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Shimaoka M., Shifman J.M., Takagi J., Mayo S.L., Springer T.A. Computational design of an integrin I domain stabilized in the open, high affinity conformation. Nat Struct Biol. 7:2000;674-678. Repacking the hydrophobic core of the αM integrin I domain to stabilize the open, high affinity conformation, or the closed, low affinity conformation.
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55
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An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
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Xiong J.-P., Li R., Essafi M., Stehle T., Arnaout M.A. An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J Biol Chem. 275:2000;38762-38767.
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56
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An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide
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Designed disulfide bonds can lock the αL integrin I domain in high or low affinity conformations.
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Lu C., Shimaoka M., Ferzly M., Oxvig C., Takagi J., Springer T.A. An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide. Proc Natl Acad Sci USA. 98:2001;2387-2392. Designed disulfide bonds can lock the αL integrin I domain in high or low affinity conformations.
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57
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0035932996
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Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin α L I domains with high affinity and antagonist activity in vivo
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Surface plasmon resonance demonstrates a 10 000-fold increase in affinity of the αL integrin for ICAM-1 when a disulfide is introduced that stabilizes the open conformation.
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Shimaoka M., Lu C., Palframan R., von Andrian U.H., Takagi J., Springer T.A. Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin α L I domains with high affinity and antagonist activity in vivo. Proc Natl Acad Sci USA. 98:2001;6009-6014. Surface plasmon resonance demonstrates a 10 000-fold increase in affinity of the αL integrin for ICAM-1 when a disulfide is introduced that stabilizes the open conformation.
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Structures of the αL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
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in press. Seven distinct disulfide bonds are introduced to stabilize alternative conformations of the αL I domain. Two have high affinity for the ligand ICAM-1, three intermediate affinity and two low affinity. High and intermediate affinity I domains are each crystallized in two distinct forms. One structure is a complex with ICAM-1. A novel intermediate conformation of I domains is revealed and the shape-shifting pathways induced by ligand binding and by pull down of the C-terminal α-helix are shown to be equivalent.
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Shimaoka M, Xiao T, Liu J-H, Yang Y, Dong Y, Jun C-D, McCormack A, Zhang R, Joachimiak A, Takagi J et al.: Structures of the αL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 2002, in press. Seven distinct disulfide bonds are introduced to stabilize alternative conformations of the αL I domain. Two have high affinity for the ligand ICAM-1, three intermediate affinity and two low affinity. High and intermediate affinity I domains are each crystallized in two distinct forms. One structure is a complex with ICAM-1. A novel intermediate conformation of I domains is revealed and the shape-shifting pathways induced by ligand binding and by pull down of the C-terminal α-helix are shown to be equivalent.
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(2002)
Cell
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Shimaoka, M.1
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Liu, J.-H.3
Yang, Y.4
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Jun, C.-D.6
McCormack, A.7
Zhang, R.8
Joachimiak, A.9
Takagi, J.10
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