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J. Biol. Chem., Vol. 269, Issue 17, 12395-12398, 04, 1994
AM Randi and N Hogg
Lymphocyte function-associated antigen-1 (LFA-1) is a beta 2 integrin that
participates in a broad range of leukocyte functions through binding to its
ligand intercellular adhesion molecule-1 (ICAM-1). The location of the
ICAM-1 binding site on LFA-1 is not known. A approximately 200-amino acid
"inserted" or "I" domain, which is part of the beta 2 integrin alpha
subunit, is homologous to the "A" domains found in the adhesive protein von
Willebrand factor and in a number of other proteins. In von Willebrand
factor, the A domains are involved in ligand binding, but their function in
the other proteins is still unclear. In this report, we show that the LFA-1
I domain contains a binding site for ICAM-1, which can be expressed as an
isolated functional unit. The I domain contains the epitopes for 18 out of
20 anti-LFA-1 monoclonal antibodies, many of which interfere with the
interaction between LFA-1 and ICAM-1. The I domain binds directly to
purified recombinant ICAM-1 and also inhibits LFA-1-dependent T cell
adhesion to ICAM-1. This report establishes the I domain as an ICAM-1
binding region in LFA-1 and the first ligand binding site to be identified
in a beta 2 integrin.
I domain of beta 2 integrin lymphocyte function-associated antigen-1 contains a binding site for ligand intercellular adhesion molecule-1
Leukocyte Adhesion Laboratory, Imperial Cancer Research Fund, London, United Kingdom.
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M. L. Bajt, T. Goodman, and S. L. McGuire beta(2)(CD18) Mutations Abolish Ligand Recognition by I Domain Integrins LFA-1 (alpha(L)beta(2), CD11a/CD18) and MAC-1 (alpha(M)beta(2), CD11b/CD18) J. Biol. Chem., January 6, 1995; 270(1): 94 - 98. [Abstract] [Full Text] [PDF]
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 D Tuckwell, D. Calderwood, L. Green, and M. Humphries Integrin alpha 2 I-domain is a binding site for collagens J. Cell Sci., January 4, 1995; 108(4): 1629 - 1637. [Abstract] [PDF]
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A. P. Mould, J. A. Askari, and M. J. Humphries Molecular Basis of Ligand Recognition by Integrin alpha 5beta 1. I. SPECIFICITY OF LIGAND BINDING IS DETERMINED BY AMINO ACID SEQUENCES IN THE SECOND AND THIRD NH2-TERMINAL REPEATS OF THE alpha SUBUNIT J. Biol. Chem., June 30, 2000; 275(27): 20324 - 20336. [Abstract] [Full Text] [PDF]
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J. M. G. Higgins, M. Cernadas, K. Tan, A. Irie, J.-h. Wang, Y. Takada, and M. B. Brenner The Role of alpha and beta Chains in Ligand Recognition by beta 7 Integrins J. Biol. Chem., August 11, 2000; 275(33): 25652 - 25664. [Abstract] [Full Text] [PDF]
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Q. Zang, C. Lu, C. Huang, J. Takagi, and T. A. Springer The Top of the Inserted-like Domain of the Integrin Lymphocyte Function-associated Antigen-1 beta Subunit Contacts the alpha Subunit beta -Propeller Domain near beta -Sheet 3 J. Biol. Chem., July 14, 2000; 275(29): 22202 - 22212. [Abstract] [Full Text] [PDF]
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P. Yalamanchili, C. Lu, C. Oxvig, and T. A. Springer Folding and Function of I Domain-deleted Mac-1 and Lymphocyte Function-associated Antigen-1 J. Biol. Chem., July 14, 2000; 275(29): 21877 - 21882. [Abstract] [Full Text] [PDF]
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E. F. Plow, T. A. Haas, L. Zhang, J. Loftus, and J. W. Smith Ligand Binding to Integrins J. Biol. Chem., July 14, 2000; 275(29): 21785 - 21788. [Full Text] [PDF]
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M. Shimaoka, C. Lu, R. T. Palframan, U. H. von Andrian, A. McCormack, J. Takagi, and T. A. Springer Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin alpha L I domains with high affinity and antagonist activity in vivo PNAS, May 22, 2001; 98(11): 6009 - 6014. [Abstract] [Full Text] [PDF]
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