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Volumn 372, Issue 1, 2003, Pages 121-127

Engineered allosteric mutants of the integrin αMβ2 I domain: Structural and functional studies

Author keywords

A domain; Allostery; Gain of function; I domain; Integrin

Indexed keywords

ADHESION; CELLS; CHEMICAL BONDS; CONFORMATIONS; CRYSTAL STRUCTURE; SURFACE PLASMON RESONANCE;

EID: 0037616465     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021273     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signalling in cell adhesion
    • Hynes, R. O. (1992) Integrins: versatility, modulation, and signalling in cell adhesion. Cell (Cambridge, Mass.) 69, 11-25
    • (1992) Cell (Cambridge, Mass.) , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 3
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the β2 intergin CR3 (CD11b/CD18) is essential for ligand binding
    • Michishita, M., Videm, V. and Arnaout, M. A. (1993) A novel divalent cation-binding site in the A domain of the β2 intergin CR3 (CD11b/CD18) is essential for ligand binding. Cell (Cambridge, Mass.) 72, 857-867
    • (1993) Cell (Cambridge, Mass.) , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 4
    • 0028075817 scopus 로고
    • Direct binding of collagen to the I-domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner
    • Kamata, T. and Takada, Y. (1994) Direct binding of collagen to the I-domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner. J. Biol. Chem. 269, 26006-26010
    • (1994) J. Biol. Chem. , vol.269 , pp. 26006-26010
    • Kamata, T.1    Takada, Y.2
  • 6
    • 0030798854 scopus 로고    scopus 로고
    • 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. and Humphries, M. J. (1997) 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, 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
  • 8
    • 0035041854 scopus 로고    scopus 로고
    • C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1
    • Takagi, J., Erickson, H. P. and Springer, T. A. (2001) C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1. Nat Struct Biol. 8, 412-416
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 412-416
    • Takagi, J.1    Erickson, H.P.2    Springer, T.A.3
  • 9
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin αIIbβ3 'inside-out' activation as regulated at its cytoplasmic face
    • Vinogradova, O., Velyvis, A., Velyviene, A., Hu, B., Haas, T., Plow, E. F. and Qin, J. (2002) A structural mechanism of integrin αIIbβ3 'inside-out' activation as regulated at its cytoplasmic face. Cell (Cambridge, Mass.) 110, 587-597
    • (2002) Cell (Cambridge, Mass.) , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.5    Plow, E.F.6    Qin, J.7
  • 10
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi, J., Petre, B. M., Walz, T. and Springer, T. A. (2002) Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell (Cambridge, Mass.) 110, 599-611
    • (2002) Cell (Cambridge, Mass.) , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 11
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz, M. A. and Ginsberg, M. H. (2002) Networks and crosstalk: integrin signalling spreads. Nat. Cell Biol. 4, E65-E68
    • (2002) Nat. Cell Biol. , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 13
    • 0028986196 scopus 로고
    • Crystal structure of the A-domain from the the α subunit of integrin CR3 (CD11b/CD18)
    • Lee, J.-O., Rieu, P., Arnaout, M. A. and Liddington, R. C. (1995) Crystal structure of the A-domain from the the α subunit of integrin CR3 (CD11b/CD18). Cell (Cambridge, Mass.) 80, 631-635
    • (1995) Cell (Cambridge, Mass.) , vol.80 , pp. 631-635
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.C.4
  • 14
    • 0028225987 scopus 로고
    • Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2, CD49b/CD29)
    • Kamata, T., Puzon, W. and Takada, Y. (1994) Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2, CD49b/CD29). J. Biol. Chem. 269, 9659-9663
    • (1994) J. Biol. Chem. , vol.269 , pp. 9659-9663
    • Kamata, T.1    Puzon, W.2    Takada, Y.3
  • 15
    • 0027933588 scopus 로고
    • The role of the I domain in ligand binding of the human integrin α1β1
    • Kern, A., Briesewitz, R., Bank, I. and Marcantonio, E. E. (1994) The role of the I domain in ligand binding of the human integrin α1β1. J. Biol. Chem. 269, 22811-22816
    • (1994) J. Biol. Chem. , vol.269 , pp. 22811-22816
    • Kern, A.1    Briesewitz, R.2    Bank, I.3    Marcantonio, E.E.4
  • 16
    • 0029059228 scopus 로고
    • Identification of amino acids in the CD11a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1)
    • Edwards, C. P., Champe, M., Gonzales, T., Wessinger, M. E., Spencer, S. A., Presta, L. G., Berman, P. W. and Bodary, S. C. (1995) Identification of amino acids in the CD11a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1). J. Biol. Chem. 270, 12635-12640
    • (1995) J. Biol. Chem. , vol.270 , pp. 12635-12640
    • Edwards, C.P.1    Champe, M.2    Gonzales, T.3    Wessinger, M.E.4    Spencer, S.A.5    Presta, L.G.6    Berman, P.W.7    Bodary, S.C.8
  • 17
    • 0029059578 scopus 로고
    • 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. and Springer, T. A. (1995) 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, 19008-19016
    • (1995) J. Biol. Chem. , vol.270 , pp. 19008-19016
    • Huang, C.1    Springer, T.A.2
  • 18
    • 0030749838 scopus 로고    scopus 로고
    • Identification and reconstruction of the binding site with in αMβ2 for a specific and high affinity ligand, NIF
    • Zhang, L. and Plow, E. F. (1997) Identification and reconstruction of the binding site with in αMβ2 for a specific and high affinity ligand, NIF. J.Biol.Chem. 272, 17558-17564
    • (1997) J. Biol. Chem. , vol.272 , pp. 17558-17564
    • Zhang, L.1    Plow, E.F.2
  • 19
    • 0032517824 scopus 로고    scopus 로고
    • Two functional states of the CD11b A-domain: Correlations with key features of two Mn2+-complexed crystal structures
    • Li, R., Rieu, P., Griffith, D. L., Scott, D. and Arnaout, M. A. (1998) Two functional states of the CD11b A-domain: correlations with key features of two Mn2+-complexed crystal structures. J. Cell Biol. 143, 1523-1534
    • (1998) J. Cell Biol. , vol.143 , pp. 1523-1534
    • Li, R.1    Rieu, P.2    Griffith, D.L.3    Scott, D.4    Arnaout, M.A.5
  • 20
    • 0033594871 scopus 로고    scopus 로고
    • Amino acid sequences within the a subunit of integrin αMβ2 (Mac-1) critical for specific recognition of C3bi
    • Zhang, L. and Plow, E. F. (1999) Amino acid sequences within the a subunit of integrin αMβ2 (Mac-1) critical for specific recognition of C3bi. Biochemistry 38, 8064-8071
    • (1999) Biochemistry , vol.38 , pp. 8064-8071
    • Zhang, L.1    Plow, E.F.2
  • 21
    • 0033527541 scopus 로고    scopus 로고
    • Interaction between collagen and the α2I-domain of integrin α2β1 - Critical role of conserved residues in the metal ion-dependent adhesion site (MIDAS) region
    • Kamata, T., Liddington, R. C. and Takada, Y. (1999) Interaction between collagen and the α2I-domain of integrin α2β1 - Critical role of conserved residues in the metal ion-dependent adhesion site (MIDAS) region. J. Biol. Chem. 274, 32108-32111
    • (1999) J. Biol. Chem. , vol.274 , pp. 32108-32111
    • Kamata, T.1    Liddington, R.C.2    Takada, Y.3
  • 22
    • 0034635523 scopus 로고    scopus 로고
    • Mapping the collagen binding site in the I domain of the glycoprotein Ia/IIa (integrin α2β1)
    • Smith, C., Estavillo, D., Emsley, J., Bankston, L., Liddington, R. C. and Cruz, M. A. (2000) Mapping the collagen binding site in the I domain of the glycoprotein Ia/IIa (integrin α2β1). J. Biol. Chem. 275, 4205-4209
    • (2000) J. Biol. Chem. , vol.275 , pp. 4205-4209
    • Smith, C.1    Estavillo, D.2    Emsley, J.3    Bankston, L.4    Liddington, R.C.5    Cruz, M.A.6
  • 24
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • Lee, J.-O., Bankston, L. A., Arnaout, M. A. and Liddington, R. C. (1995) Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure 3, 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
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 84920325457 scopus 로고
    • AMORE - An atomated molecular replacement program package
    • Navaza, J. (1994) AMORE - an atomated molecular replacement program package. Acta Cryst. A50, 157-163
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. and Schneider, T. (1997) SHELXL: High-resolution refinement. Methods Enzymol. 277, 319-343
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.1    Schneider, T.2
  • 30
    • 0033515012 scopus 로고    scopus 로고
    • Conformational changes in tertiary structure near the ligand binding site of an integrin I domain
    • Oxvig, C., Lu, C. and Springer, T. A. (1999) Conformational changes in tertiary structure near the ligand binding site of an integrin I domain. Proc. Natl. Acad. Sci. U.S.A. 96, 2215-2220
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2215-2220
    • Oxvig, C.1    Lu, C.2    Springer, T.A.3
  • 31
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • Xiong, J. P., Li, R., Essafi, M., Stehle, T. and Arnaout, M. A. (2000) An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J. Biol. Chem. 275, 38762-38767
    • (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
  • 33
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulphide bond: Integrin αL I domains with high affinity and antagonist activity in vivo
    • Shimaoka, M., Lu, C., Palframan, R. T., von Andrian, U. H., McCormack, A., Takagi, J. and Springer, T. A. (2001) Reversibly locking a protein fold in an active conformation with a disulphide bond: integrin αL I domains with high affinity and antagonist activity in vivo. Proc. Natl. Acad. Sci. U.S.A. 98, 6009-6014
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.T.3    Von Andrian, U.H.4    McCormack, A.5    Takagi, J.6    Springer, T.A.7
  • 34
    • 0029977944 scopus 로고    scopus 로고
    • A discrete site modulates activation of I domains
    • Zhang, L. and Plow, E. F. (1996) A discrete site modulates activation of I domains. J. Biol. Chem. 271, 29953-29957
    • (1996) J. Biol. Chem. , vol.271 , pp. 29953-29957
    • Zhang, L.1    Plow, E.F.2
  • 35
    • 0035422428 scopus 로고    scopus 로고
    • Cellular activation of leukocyte function-associated antigen-1 and its affinity are regulated at the I domain allosteric site
    • Lupher, M. L. J., Harris, E. A., Beals, C. R., Sui, L. M., Liddington, R. C. and Staunton, D. E. (2001) Cellular activation of leukocyte function-associated antigen-1 and its affinity are regulated at the I domain allosteric site. J. Immunol. 167, 1431-1439
    • (2001) J. Immunol. , vol.167 , pp. 1431-1439
    • Lupher, M.L.J.1    Harris, E.A.2    Beals, C.R.3    Sui, L.M.4    Liddington, R.C.5    Staunton, D.E.6
  • 36
    • 0037076494 scopus 로고    scopus 로고
    • Does the Integrin alphaA domain act as a ligand for its betaA domain?
    • Alonso, J. L., Essafi, M., Xiong, J. P., Stehle, T. and Arnaout, M. A. (2002) Does the Integrin alphaA domain act as a ligand for its betaA domain? Curr. Biol. 12, R340-R342
    • (2002) Curr. Biol. , vol.12
    • Alonso, J.L.1    Essafi, M.2    Xiong, J.P.3    Stehle, T.4    Arnaout, M.A.5
  • 37
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • Liddington, R. C. and Ginsberg, M. H. (2002) Integrin activation takes shape. J. Cell Biol. 158, 833-839
    • (2002) J. Cell Biol. , vol.158 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.