Direct binding of collagen to the I domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner

Tetsuji Kamata, Yoshikazu Takada

Research output: Contribution to journalArticle

136 Citations (Scopus)

Abstract

Integrin α2β1 is a major divalent cation-dependent receptor for collagen. Here, we show that the recombinant inserted/interactive domain (I domain) of α2 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 α2β1 and the I domain fragment. Thr-221 may be involved in the actual collagen binding and recognition.

Original languageEnglish
Pages (from-to)26006-26010
Number of pages5
JournalJournal of Biological Chemistry
Volume269
Issue number42
Publication statusPublished - 1994 Oct 21
Externally publishedYes

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Integrin alpha2beta1
Divalent Cations
Integrins
Collagen
Collagen Receptors
Ligands

ASJC Scopus subject areas

  • Biochemistry

Cite this

Direct binding of collagen to the I domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner. / Kamata, Tetsuji; Takada, Yoshikazu.

In: Journal of Biological Chemistry, Vol. 269, No. 42, 21.10.1994, p. 26006-26010.

Research output: Contribution to journalArticle

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