Figure 1. Model for affinity modulation of integrins. (a) Schematic diagram depicting the arrangement of domains within an I-domain-containing integrin. The integrin is in an inactive bent conformation. (b,c) Ribbon diagrams depicting the bent inactive conformation of the extracellular portion of an integrin (b), and the extended conformation of the extracellular protein of an activated integrin (c). Black bar indicates 100 Å. Reprinted from Cell, 110, Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. 599–611, Copyright (2002), with permission from Elsevier.

Figure 2. Sequence alignment of human integrin subunit (a), and subunit (b) cytoplasmic domains. Highly conserved amino acid residues are highlighted, and provided as a consensus below the alignments.

Figure 3. (a–c) Modes of regulation of intracellular signal transduction cascades by integrins and crosstalk with other transmembrane receptors.