Chapter category: Adhesion Molecules
Structural Aspects of Integrins
I Domains in Integrins
Edited by: Donald GullbergISBN: 0-306-47836-6
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Chapter authors:
Robert C. Liddington
Structural studies on integrins have recently made great strides. In the past three years, crystal structures of the complete extracellular fragment of one integrin, aVb3,1 two a-I domains in complex with ligands,2,3 and an intracellular activating protein in complex with a b tail4 have been obtained; and an ab tail complex has been determined by NMR.5 High resolution EM studies complement these atomic resolution techniques by studying the integrin in different activation states.6,7 Although we have only a few experimental examples among integrin family members, the high level of sequence homology between integrins means that reliable models can be built of the other members of the integrin family. These structures make sense of a lot of preceding biochemical, biophysical and mutagenesis studies, and generate many new testable hypotheses of integrin function. This chapter emphasizes new structural insights applicable to all integrins, with an emphasis on those integrins that contain an a-I domain. The structural data reinforce the notion of the integrin as a molecule in dynamic equilibrium at the cell surface, regulated by binding both to extracellular and intracellular ligands.
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Structural Aspects of Integrins
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Structural studies on integrins have recently made great strides. In the past three years, crystal structures of the complete extracellular fragment of one integrin, a
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Evolution of Integrin I-Domains
Mark S. Johnson and Danny Tuckwell
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
