PMID: 9543001May 23, 1998Paper

Development of a structural model for the cytoplasmic domain of an integrin

Protein Engineering
T A Haas, E F Plow

Abstract

The cytoplasmic tails of integrin heterodimers play central roles in controlling the activation states of integrins and in transmitting intracellular signals. Despite their short length, no structure of any integrin cytoplasmic domain has been determined. Therefore, molecular models for the cytoplasmic domain of alpha(IIb)beta3, the major platelet integrin, were generated, including models for the individual cytoplasmic tails, the binary alphaIIb-calcium complex, and the ternary alphaIIb-beta3-calcium complex. Structural analysis of circular dichroism spectra were compiled with data obtained from short homologous sequences within crystallized proteins, and with secondary structural predictions to develop starting models for each subunit. These models were subjected to a series of energy minimization and molecular dynamic simulations to generate final models. AlphaIIb was predicted to be ordered at its N-terminus and its C-terminus could accommodate a cation in a multicoordinated complex. The structure of beta3 was dominated by a beta-turn at its NPXY motif (beta3 744-747). In docking of alphaIIb to different sites within beta3, the conformation of the beta3 juxta-transmembrane (beta3 716-721) was greatly altered. This region wa...Continue Reading

Citations

Jun 29, 2004·Micron : the International Research and Review Journal for Microscopy·Mohammad A Hussain, Christopher A Siedlecki
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Sep 21, 2002·Molecular and Cellular Endocrinology·Tae-Yon ChunJ Howard Pratt
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