-
1
-
-
0028986196
-
Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18)
-
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.
-
(1995)
Cell
, vol.80
, pp. 631-638
-
-
Lee, J.O.1
Rieu, P.2
Arnaout, M.A.3
Liddington, R.4
-
2
-
-
0035850669
-
Crystal structure of the extracellular segment of integrin αVβ3
-
This is the first report of the crystal structure of a full-length extracellular integrin dimer. The coordinates provide the structural template onto which functional sites are mapped in this article.
-
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 This is the first report of the crystal structure of a full-length extracellular integrin dimer. The coordinates provide the structural template onto which functional sites are mapped in this article.
-
(2001)
Science
, vol.294
, pp. 339-345
-
-
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
-
3
-
-
0037023363
-
Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
-
This is the first report of the crystal structure of a full-length extracellular integrin dimer complexed with a ligand. The RGD contact sites validate much of the data described in this review.
-
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. 296:2002;151-155 This is the first report of the crystal structure of a full-length extracellular integrin dimer complexed with a ligand. The RGD contact sites validate much of the data described in this review.
-
(2002)
Science
, vol.296
, pp. 151-155
-
-
Xiong, J.P.1
Stehle, T.2
Zhang, R.3
Joachimiak, A.4
Frech, M.5
Goodman, S.L.6
Arnaout, M.A.7
-
6
-
-
0037145037
-
Integrins: Bidirectional, allosteric signaling machines
-
Hynes R. Integrins: bidirectional, allosteric signaling machines. Cell. 110:2002;673-687.
-
(2002)
Cell
, vol.110
, pp. 673-687
-
-
Hynes, R.1
-
8
-
-
0013264177
-
Integrin structure: Heady advances in ligand binding, but activation makes the knees wobble
-
in press
-
Humphries MJ, McEwan PA, Askari JA, Barton SJ, Buckley PA, Craig SE, Bella J, Mould AP: Integrin structure: heady advances in ligand binding, but activation makes the knees wobble. Trends Biochem Sci 2003, in press.
-
(2003)
Trends Biochem Sci
-
-
Humphries, M.J.1
McEwan, P.A.2
Askari, J.A.3
Barton, S.J.4
Buckley, P.A.5
Craig, S.E.6
Bella, J.7
Mould, A.P.8
-
10
-
-
0034233731
-
Genetic analysis of integrin function in man: LAD-1 and other syndromes
-
Hogg N., Bates P.A. Genetic analysis of integrin function in man: LAD-1 and other syndromes. Matrix Biol. 19:2000;211-222.
-
(2000)
Matrix Biol.
, vol.19
, pp. 211-222
-
-
Hogg, N.1
Bates, P.A.2
-
11
-
-
0031929048
-
The molecular genetics of Glanzmann's thrombasthenia
-
French D.L. The molecular genetics of Glanzmann's thrombasthenia. Platelets. 9:1998;5-20.
-
(1998)
Platelets
, vol.9
, pp. 5-20
-
-
French, D.L.1
-
12
-
-
0026028144
-
Further studies on the topography of the N-terminal region of human platelet glycoprotein IIIa. Localization of monoclonal antibody epitopes and the putative fibrinogen-binding sites
-
Calvete J.J., Arias J., Alvarez M.V., Lopez M.M., Henschen A., Gonzalez-Rodriguez J. Further studies on the topography of the N-terminal region of human platelet glycoprotein IIIa. Localization of monoclonal antibody epitopes and the putative fibrinogen-binding sites. Biochem. J. 274:1991;457-463.
-
(1991)
Biochem. J.
, vol.274
, pp. 457-463
-
-
Calvete, J.J.1
Arias, J.2
Alvarez, M.V.3
Lopez, M.M.4
Henschen, A.5
Gonzalez-Rodriguez, J.6
-
13
-
-
0026086681
-
Further studies on the topography of human platelet glycoprotein IIb. Localization of monoclonal antibody epitopes and the putative glycoprotein IIa- and fibrinogen-binding regions
-
Calvete J.J., Arias J., Alvarez M.V., Lopez M.M., Henschen A., Gonzalez-Rodriguez J. Further studies on the topography of human platelet glycoprotein IIb. Localization of monoclonal antibody epitopes and the putative glycoprotein IIa- and fibrinogen-binding regions. Biochem. J. 273:1991;767-775.
-
(1991)
Biochem. J.
, vol.273
, pp. 767-775
-
-
Calvete, J.J.1
Arias, J.2
Alvarez, M.V.3
Lopez, M.M.4
Henschen, A.5
Gonzalez-Rodriguez, J.6
-
14
-
-
0027248518
-
Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies
-
Takada Y., Puzon W. Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268:1993;17597-17601.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 17597-17601
-
-
Takada, Y.1
Puzon, W.2
-
15
-
-
0027990819
-
Mutation of a ligand binding domain of β3 integrin. Integral role of oxygenated residues in αIIbβ3 (GPIIb-IIIa) receptor function
-
Bajt M.L., Loftus J.C. Mutation of a ligand binding domain of β3 integrin. Integral role of oxygenated residues in αIIbβ3 (GPIIb-IIIa) receptor function. J. Biol. Chem. 269:1994;20913-20919.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 20913-20919
-
-
Bajt, M.L.1
Loftus, J.C.2
-
16
-
-
0028225987
-
Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2 CD49b/CD29)
-
Kamata T., Puzon W., Takada Y. Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2 CD49b/CD29). J. Biol. Chem. 269:1994;9659-9663.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 9659-9663
-
-
Kamata, T.1
Puzon, W.2
Takada, Y.3
-
17
-
-
0028805249
-
Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third N-terminal repeat in the integrin α4 and α5 subunits
-
Irie A., Kamata T., Puzon-McLaughlin W., Takada Y. Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third N-terminal repeat in the integrin α4 and α5 subunits. EMBO J. 14:1995;5550-5556.
-
(1995)
EMBO J.
, vol.14
, pp. 5550-5556
-
-
Irie, A.1
Kamata, T.2
Puzon-McLaughlin, W.3
Takada, Y.4
-
18
-
-
0028900673
-
Identification of putative ligand-binding sites of the integrin α4β1 (VLA-4, CD49d/CD29)
-
Kamata T., Puzon W., Takada Y. Identification of putative ligand-binding sites of the integrin α4β1 (VLA-4, CD49d/CD29). Biochem. J. 305:1995;945-951.
-
(1995)
Biochem. J.
, vol.305
, pp. 945-951
-
-
Kamata, T.1
Puzon, W.2
Takada, Y.3
-
19
-
-
0029059578
-
A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)
-
Huang C., Springer T.A. A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1). J. Biol. Chem. 270:1995;19008-19016.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 19008-19016
-
-
Huang, C.1
Springer, T.A.2
-
20
-
-
0029015716
-
Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi
-
Kamata T., Wright R., Takada Y. Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi. J. Biol. Chem. 270:1995;12531-12535.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 12531-12535
-
-
Kamata, T.1
Wright, R.2
Takada, Y.3
-
21
-
-
0029060141
-
Molecular mapping of functional antibody binding sites of α4 integrin
-
Schiffer S.G., Hemlers M.E., Lobb R.R., Tizard R., Osborn L. Molecular mapping of functional antibody binding sites of α4 integrin. J. Biol. Chem. 270:1995;14270-14273.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 14270-14273
-
-
Schiffer, S.G.1
Hemlers, M.E.2
Lobb, R.R.3
Tizard, R.4
Osborn, L.5
-
22
-
-
0029780525
-
Critical residues of integrin αIIb subunit for binding of αIIbβ3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3)
-
Kamata T., Irie A., Tokuhira M., Takada Y. Critical residues of integrin αIIb subunit for binding of αIIbβ3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J. Biol. Chem. 271:1996;18610-18615.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 18610-18615
-
-
Kamata, T.1
Irie, A.2
Tokuhira, M.3
Takada, Y.4
-
23
-
-
0029671448
-
A region of the integrin VLA α4 subunit involved in homotypic cell aggregation and in fibronectin but not vascular cell adhesion molecule-1 binding
-
Munoz M., Serrador J., Sanchez-Madrid F., Teixido J. A region of the integrin VLA α4 subunit involved in homotypic cell aggregation and in fibronectin but not vascular cell adhesion molecule-1 binding. J. Biol. Chem. 271:1996;2696-2702.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 2696-2702
-
-
Munoz, M.1
Serrador, J.2
Sanchez-Madrid, F.3
Teixido, J.4
-
24
-
-
0029786408
-
Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit
-
Puzon-McLaughlin W., Takada Y. Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit. J. Biol. Chem. 271:1996;20438-20443.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 20438-20443
-
-
Puzon-McLaughlin, W.1
Takada, Y.2
-
25
-
-
0030669061
-
A novel region of the α4 integrin subunit with a modulatory role in VLA-4-mediated cell adhesion to fibronectin
-
Munoz M., Serrador J., Nieto M., Luque A., Sanchez-Madrid F., Teixido J. A novel region of the α4 integrin subunit with a modulatory role in VLA-4-mediated cell adhesion to fibronectin. Biochem. J. 327:1997;727-733.
-
(1997)
Biochem. J.
, vol.327
, pp. 727-733
-
-
Munoz, M.1
Serrador, J.2
Nieto, M.3
Luque, A.4
Sanchez-Madrid, F.5
Teixido, J.6
-
26
-
-
0032582542
-
Mapping the intercellular adhesion molecule-1 and -2 binding site on the inserted domain of leukocyte function-associated antigen-1
-
Edwards C.P., Fisher K.L., Presta L.G., Bodary S.C. Mapping the intercellular adhesion molecule-1 and -2 binding site on the inserted domain of leukocyte function-associated antigen-1. J. Biol. Chem. 273:1998;28937-28944.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 28937-28944
-
-
Edwards, C.P.1
Fisher, K.L.2
Presta, L.G.3
Bodary, S.C.4
-
27
-
-
0033406615
-
Fine mapping of inhibitory anti-α5 monoclonal antibody epitopes that differentially affect integrin-ligand binding
-
Burrows L., Clark K., Mould A.P., Humphries M.J. Fine mapping of inhibitory anti-α5 monoclonal antibody epitopes that differentially affect integrin-ligand binding. Biochem. J. 344:1999;527-533.
-
(1999)
Biochem. J.
, vol.344
, pp. 527-533
-
-
Burrows, L.1
Clark, K.2
Mould, A.P.3
Humphries, M.J.4
-
28
-
-
0033527541
-
Interaction between collagen and the alpha(2) I-domain of integrin alpha(2)beta(1). Critical role of conserved residues in the metal ion-dependent adhesion site (MIDAS) region
-
Kamata T., Liddington R.C., Takada Y. Interaction between collagen and the alpha(2) I-domain of integrin alpha(2)beta(1). Critical role of conserved residues in the metal ion-dependent adhesion site (MIDAS) region. J. Biol. Chem. 274:1999;32108-32111.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 32108-32111
-
-
Kamata, T.1
Liddington, R.C.2
Takada, Y.3
-
29
-
-
0033594871
-
Amino acid sequences within the alpha subunit of integrin alpha M beta 2 (Mac-1) critical for specific recognition of C3bi
-
Zhang L., Plow E.F. Amino acid sequences within the alpha subunit of integrin alpha M beta 2 (Mac-1) critical for specific recognition of C3bi. Biochemistry. 38:1999;8064-8071.
-
(1999)
Biochemistry
, vol.38
, pp. 8064-8071
-
-
Zhang, L.1
Plow, E.F.2
-
30
-
-
2542507763
-
Integrin alpha(2)I domain recognizes type I and type IV collagens by different mechanisms
-
Kapyla J., Ivaska J., Riikonen R., Nykvist P., Pentikainen O., Johnson M., Heino J. Integrin alpha(2)I domain recognizes type I and type IV collagens by different mechanisms. J. Biol. Chem. 275:2000;3348-3354.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 3348-3354
-
-
Kapyla, J.1
Ivaska, J.2
Riikonen, R.3
Nykvist, P.4
Pentikainen, O.5
Johnson, M.6
Heino, J.7
-
31
-
-
0035941265
-
Amino acid residues in the αIIb subunit that are critical for ligand binding to integrin αIIbβ3 are clustered in the beta-propeller model
-
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 beta-propeller model. J. Biol. Chem. 276:2001;44275-44283.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 44275-44283
-
-
Kamata, T.1
Tieu, K.K.2
Springer, T.A.3
Takada, Y.4
-
32
-
-
0035377569
-
Structure-function of the putative I-domain within the integrin β2 subunit
-
Xiong Y., Zhang L. Structure-function of the putative I-domain within the integrin β2 subunit. J. Biol. Chem. 276:2001;19340-19349.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 19340-19349
-
-
Xiong, Y.1
Zhang, L.2
-
33
-
-
0034737296
-
Structural basis of collagen recognition by integrin alpha2beta1
-
The first report of the crystal structure of an integrin domain complexed with its ligand. The coordinates provide the template for transposing functional sites within αA-domains.
-
Emsley J., Knight C.G., Farndale R.W., Barnes M.J., Liddington R.C. Structural basis of collagen recognition by integrin alpha2beta1. Cell. 101:2000;47-56 The first report of the crystal structure of an integrin domain complexed with its ligand. The coordinates provide the template for transposing functional sites within αA-domains.
-
(2000)
Cell
, vol.101
, pp. 47-56
-
-
Emsley, J.1
Knight, C.G.2
Farndale, R.W.3
Barnes, M.J.4
Liddington, R.C.5
-
34
-
-
0037428080
-
Structures of the αL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
-
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. 112:2003;99-111.
-
(2003)
Cell
, vol.112
, pp. 99-111
-
-
Shimaoka, M.1
Xiao, T.2
Liu, J.H.3
Yang, Y.4
Dong, Y.5
Jun, C.D.6
McCormack, A.7
Zhang, R.8
Joachimiak, A.9
Takagi, J.10
-
35
-
-
0033982205
-
Integrin cell adhesion receptors and the concept of agonism
-
Humphries M.J. Integrin cell adhesion receptors and the concept of agonism. Trends Pharmacol. Sci. 21:2000;29-32.
-
(2000)
Trends Pharmacol. Sci.
, vol.21
, pp. 29-32
-
-
Humphries, M.J.1
-
36
-
-
0028985252
-
β2 (CD18) mutations abolish ligand recognition by I domain integrins LFA- 1 (αLβ2, CD11a/CD18) and MAC-1 (αMβ2, CD11b/CD18)
-
Bajt M.L., Goodman T., McGuire S.L. β2 (CD18) mutations abolish ligand recognition by I domain integrins LFA- 1 (αLβ2, CD11a/CD18) and MAC-1 (αMβ2, CD11b/CD18). J. Biol. Chem. 270:1995;94-98.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 94-98
-
-
Bajt, M.L.1
Goodman, T.2
McGuire, S.L.3
-
37
-
-
0036220127
-
Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
-
This paper reports the NMR solution structure of the EGF3 repeat and the EGF2-EGF3 junction at the knee of the β2 subunit. The structure reveals the sites of activating mutations and stimulatory mAb epitopes within β2, and suggests a switchblade model of receptor opening that leads to activation.
-
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 This paper reports the NMR solution structure of the EGF3 repeat and the EGF2-EGF3 junction at the knee of the β2 subunit. The structure reveals the sites of activating mutations and stimulatory mAb epitopes within β2, and suggests a switchblade model of receptor opening that leads to activation.
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 282-287
-
-
Beglova, N.1
Blacklow, S.C.2
Takagi, J.3
Springer, T.A.4
-
38
-
-
0034617217
-
Molecular basis of ligand recognition by integrin α5β1: Specificity of ligand binding is determined by amino acid sequences in the second and third NH2-terminal repeats of the α subunit
-
Mould P., Askari J.A., Humphries M.J. Molecular basis of ligand recognition by integrin α5β1: specificity of ligand binding is determined by amino acid sequences in the second and third NH2-terminal repeats of the α subunit. J. Biol. Chem. 275:2000;20324-20336.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 20324-20336
-
-
Mould, P.1
Askari, J.A.2
Humphries, M.J.3
-
39
-
-
0034678063
-
Multiple discontinuous ligand-mimetic antibody binding sites define a ligand binding pocket in integrin alpha(IIb)beta(3)
-
Puzon-McLaughlin W., Kamata T., Takada Y. Multiple discontinuous ligand-mimetic antibody binding sites define a ligand binding pocket in integrin alpha(IIb)beta(3). J. Biol. Chem. 275:2000;7795-7802.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 7795-7802
-
-
Puzon-McLaughlin, W.1
Kamata, T.2
Takada, Y.3
-
40
-
-
0030798854
-
Defining the topology of integrin α5β1- fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies. Evidence that the synergy sequence of fibronectin is recognized by the amino-terminal repeats of the α5 subunit
-
Mould A.P., Askari J.A., Aota S., Yamada K.M., Irie A., Takada Y., Mardon H.J., Humphries M.J. Defining the topology of integrin α5β1- fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies. Evidence that the synergy sequence of fibronectin is recognized by the amino-terminal repeats of the α5 subunit. J. Biol. Chem. 272:1997;17283-17292.
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 17283-17292
-
-
Mould, A.P.1
Askari, J.A.2
Aota, S.3
Yamada, K.M.4
Irie, A.5
Takada, Y.6
Mardon, H.J.7
Humphries, M.J.8
-
41
-
-
0029664954
-
The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy. Evidence for allosteric inhibition of integrin function
-
Mould A.P., Akiyama S.K., Humphries M.J. The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy. Evidence for allosteric inhibition of integrin function. J. Biol. Chem. 271:1996;20365-20374.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 20365-20374
-
-
Mould, A.P.1
Akiyama, S.K.2
Humphries, M.J.3
-
42
-
-
0032080651
-
Analysis of ligand-induced and ligand-attenuated epitopes on the leukocyte integrin α4β1: VCAM-1, mucosal addressin cell adhesion molecule-1, and fibronectin induce distinct conformational changes
-
Newham P., Craig S.E., Clark K., Mould A.P., Humphries M.J. Analysis of ligand-induced and ligand-attenuated epitopes on the leukocyte integrin α4β1: VCAM-1, mucosal addressin cell adhesion molecule-1, and fibronectin induce distinct conformational changes. J. Immunol. 160:1998;4508-4517.
-
(1998)
J. Immunol.
, vol.160
, pp. 4508-4517
-
-
Newham, P.1
Craig, S.E.2
Clark, K.3
Mould, A.P.4
Humphries, M.J.5
-
43
-
-
0032475978
-
Identification of amino acid residues that form part of the ligand-binding pocket of integrin α5β1
-
Mould A.P., Burrows L., Humphries M.J. Identification of amino acid residues that form part of the ligand-binding pocket of integrin α5β1. J. Biol. Chem. 273:1998;25664-25672.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 25664-25672
-
-
Mould, A.P.1
Burrows, L.2
Humphries, M.J.3
-
44
-
-
0029646107
-
Two conformations of the integrin A-domain (I-domain): A pathway for activation?
-
Lee J.O., Bankston L.A., Arnaout M.A., Liddington R.C. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure. 3:1995;1333-1340.
-
(1995)
Structure
, vol.3
, pp. 1333-1340
-
-
Lee, J.O.1
Bankston, L.A.2
Arnaout, M.A.3
Liddington, R.C.4
-
45
-
-
0034624058
-
An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
-
Either mutation or deletion of an invariant isoleucine residue in the C-terminal helix of the αM A-domain was shown to activate ligand binding constitutively. The isoleucine fits into a hydrophobic pocket in the closed conformation of the A-domain, but is exposed in the open form. This transition appears to be a key feature of the activation process as it is coupled to both structural rearrangements at the MIDAS (metal-ion-dependent adhesion site) site and a downward movement of the C-terminal α7 helix.
-
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 Either mutation or deletion of an invariant isoleucine residue in the C-terminal helix of the αM A-domain was shown to activate ligand binding constitutively. The isoleucine fits into a hydrophobic pocket in the closed conformation of the A-domain, but is exposed in the open form. This transition appears to be a key feature of the activation process as it is coupled to both structural rearrangements at the MIDAS (metal-ion-dependent adhesion site) site and a downward movement of the C-terminal α7 helix.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 38762-38767
-
-
Xiong, J.P.1
Li, R.2
Essafi, M.3
Stehle, T.4
Arnaout, M.A.5
-
46
-
-
0034625083
-
NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding
-
Huth J.R., Olejniczak E.T., Mendoza R., Liang H., Harris E.A., Lupher M.L., Wilson A.E., Fesik S.W., Staunton D.E. NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding. Proc. Natl. Acad Sci. USA. 97:2000;5231-5236.
-
(2000)
Proc. Natl. Acad Sci. USA
, vol.97
, pp. 5231-5236
-
-
Huth, J.R.1
Olejniczak, E.T.2
Mendoza, R.3
Liang, H.4
Harris, E.A.5
Lupher, M.L.6
Wilson, A.E.7
Fesik, S.W.8
Staunton, D.E.9
-
47
-
-
0013307787
-
Conformational changes in the integrin βA-domain provide a mechanism for signal transduction via hybrid domain movement
-
in press
-
Mould AP, Barton SJ, Askari JA, McEwan PA, Buckley PA, Craig SE, Humphries MJ: Conformational changes in the integrin βA-domain provide a mechanism for signal transduction via hybrid domain movement. J Biol Chem 2003, in press.
-
(2003)
J Biol Chem
-
-
Mould, A.P.1
Barton, S.J.2
Askari, J.A.3
McEwan, P.A.4
Buckley, P.A.5
Craig, S.E.6
Humphries, M.J.7
-
48
-
-
0037031906
-
Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
-
2+ results in an extended structure coupled to an outward swing of the hybrid domain at its junction with the βA-domain.
-
2+ results in an extended structure coupled to an outward swing of the hybrid domain at its junction with the βA-domain.
-
(2002)
Cell
, vol.110
, pp. 599-611
-
-
Takagi, J.1
Petre, B.2
Walz, T.3
Springer, T.4
-
49
-
-
0037205483
-
Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain
-
Mould A.P., Askari J.A., Barton S., Kline A.D., McEwan P.A., Craig S.E., Humphries M.J. Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain. J. Biol. Chem. 277:2002;19800-19805.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 19800-19805
-
-
Mould, A.P.1
Askari, J.A.2
Barton, S.3
Kline, A.D.4
McEwan, P.A.5
Craig, S.E.6
Humphries, M.J.7
-
50
-
-
0033543673
-
Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain
-
Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G., Cottens S., Weitz-Schmidt G., Hommel U. Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain. J. Mol. Biol. 292:1999;1-9.
-
(1999)
J. Mol. Biol.
, vol.292
, pp. 1-9
-
-
Kallen, J.1
Welzenbach, K.2
Ramage, P.3
Geyl, D.4
Kriwacki, R.5
Legge, G.6
Cottens, S.7
Weitz-Schmidt, G.8
Hommel, U.9
|