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Cysteine-rich region

Cysteine-rich region

Figure 1 The domain structure of integrin heterodimers. The u and (3 subunits both contain the highlighted MIDAS (metal ion-dependent adhesion site) motif. Domains V-VII In I domain containing integrins (or IV—VH in others) have EF hand-like cation-binding sequences with a conserved motif DxDxDxxxDxxx (X is any amino acid). The positions of ligand-binding domains for ICAM-1 within aLp2 are indicated as y////s. The (3-subunit cytoplasmic domain insert shows the two conserved NPXY/F motifs present in all f> subunits except (i4 and (J8. The first NPXY motif has been shown to be important for affinity changes in (J, and p3. The TTT motif in p2 regulates adhesion through postreceptor events. TM, transmembrane sequence. (Reproduced with permission from Stewart et al. (1995).)

Figure 1 The domain structure of integrin heterodimers. The u and (3 subunits both contain the highlighted MIDAS (metal ion-dependent adhesion site) motif. Domains V-VII In I domain containing integrins (or IV—VH in others) have EF hand-like cation-binding sequences with a conserved motif DxDxDxxxDxxx (X is any amino acid). The positions of ligand-binding domains for ICAM-1 within aLp2 are indicated as y////s. The (3-subunit cytoplasmic domain insert shows the two conserved NPXY/F motifs present in all f> subunits except (i4 and (J8. The first NPXY motif has been shown to be important for affinity changes in (J, and p3. The TTT motif in p2 regulates adhesion through postreceptor events. TM, transmembrane sequence. (Reproduced with permission from Stewart et al. (1995).)

an area of high homology which is thought to participate in a|3 heterodimer formation and in ligand binding. Secondary structure prediction provides convincing evidence that this domain is homologous to the I domain of the a subunit, suggesting that seven integrins have two I domains, whereas the remainder have only the single I domain of the P subunit. More C terminal to this region, the p sub-units have another distinctive feature in the positioning of 37 cysteines within a restricted area of 190 amino acids, giving rise to extensive disulfide bonding. Electron microscopic analysis of ct5(3, reveals a mushroom-shaped globular 'head', containing the ligand-binding area, supported on the membrane by 'stalks' formed by the C-terminal regions of the a subunit and the rigidly cross-linked p subunit.

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