Analysis of the Binding Site on Intercellular Adhesion Molecule 3 for the Leukocyte Integrin Lymphocyte Function-associated Antigen 1
| Autor: | David Simmons, Amanda J. Littler, Claire L. Holness, Alison McDowall, Nancy Hogg, Paul A. Bates, David Bossy, Christopher D. Buckley |
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| Rok vydání: | 1995 |
| Předmět: |
Models
Molecular Molecular Sequence Data Integrin CD18 Biochemistry Cell Line Antigens CD Animals Humans Amino Acid Sequence Lymphocyte function-associated antigen 1 Molecular Biology DNA Primers ICAM3 Binding Sites ICAM2 COS cells Base Sequence Sequence Homology Amino Acid biology Cell Biology Intercellular adhesion molecule Antigens Differentiation Molecular biology Lymphocyte Function-Associated Antigen-1 Cell biology Mutagenesis Site-Directed biology.protein Immunoglobulin superfamily Cell Adhesion Molecules |
| Zdroj: | Journal of Biological Chemistry. 270:877-884 |
| ISSN: | 0021-9258 |
| Popis: | Intercellular adhesion molecule 3 (ICAM-3, CD50) is a member of the immunoglobulin superfamily and is a constitutively expressed ligand for the leukocyte integrin LFA-1 (CD11a/CD18). ICAM-3 is expressed at high levels by all resting leukocyte populations and antigen presenting cells and is a major ligand for LFA-1 in the resting immune system. ICAM-3 is a signal transducer and may play a key role in initiating immune responses. Mutant ICAM-3 Fc-chimeric proteins were quantitatively analyzed for their ability to bind COS cells expressing human LFA-1. The LFA-1-binding site on ICAM-3 is located in the N-terminal 2 Ig domains. Domains 3-5 do not significantly contribute to adhesion. The binding site has been further resolved by rational targeting of 14 point mutations throughout domains 1 and 2, coupled with modeling studies. Within domain 1 a cluster of residues (Glu 37 , Leu 66 , Ser 68 , and Gln 75 ), that are predicted to lie on the CC′FG face of the Ig fold, play a dominant role in LFA-1 binding. |
| Databáze: | OpenAIRE |
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