Chapter category: Adhesion Molecules
Integrin Recognition Motifs in Collagens
I Domains in Integrins
Edited by: Donald GullbergISBN: 0-306-47836-6
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Chapter authors:
Richard W. Farndale
The vertebrate integrins are a family of twenty four heterodimeric transmembrane sig nalling and adhesion molecules, found in very many cells types where their expression and affinity is carefully regulated, reviewed in Chapter 1 and.1,2 Integrins mediate either cell–cell interactions, often with cellular adhesion molecules (CAMs) as counter-receptors,3 or cell–matrix interactions.4 The two matrix molecules best-known in the latter context are fibronectin and collagen. Fibronectin is a ligand for both b1 and b3 integrins, with a5b1 as its most widespread receptor, whereas collagen is considered to interact directly only with a subset of the b1 integrins which is characterised by the presence within the a–subunit of an inserted, or I, domain. For a recent review, see.5 The a-I domain adopts the dinucleotide-binding, or Rossman, fold, compared in.6 This structure, the prototype for which is the von Willebrand factor A–domain, is found in intracellular signalling species such as G protein a–subunits and in extracellular adhesive proteins including the terminal extensions of the non-fibrillar collagens. 7 Under physiological conditions, the integrin a-I domains, though not necessarily other A-domains,8 constitutively bind a divalent cation, Mg2+, in their metal ion dependent adhesion site (MIDAS) which is the focus of their interaction with collagens.9 Of the four collagen-binding integrins, a1b1 and a2b1 have been studied for over a decade10-25 whilst the properties of both a10b1, which was purified using its capacity to bind collagen II26-28 and a11b129-31 are just beginning to receive attention. Data is emerging to suggest differential ability of a10a1 and a11a1, like that of a1a1 and a2b1, to interact with specific collagen types.32,33
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Evolution of Integrin I-Domains
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In humans, I domains are ~200 residue long sequences that are “inserted” into the N-terminal domain of all 8 integrin a subunits and 9 of the 18 integrin
