Work

Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner

Year: 1994

Type: article

Abstract: Integrin alpha 2 beta 1 is a major divalent cation-dependent receptor for collagen. Here, we show that the recombinant inserted/interactive domain (I domain) of alpha 2 specifically interacts with collagen, indicating the I domain contains all the components necessary for collagen binding. Evidence was obtained that divalent cations are not required for collagen binding to the I domain fragment, indicating that divalent cations are not involved in the actual binding to collagen but probably in the regulation of the binding. We identified Thr-221 within the previously identified putative ligand binding region as a residue critical for collagen binding to both alpha 2 beta 1 and the I domain fragment. Thr-221 may be involved in the actual collagen binding and recognition.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)47151-7

Authors: T Kamata, Y Takada

Institution: Scripps Research Institute

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funder: National Institute of General Medical Sciences