Purification, analysis, and crystal structure of integrins
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Updated: Jul 13, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Jian-Ping Xiong1, Simon L Goodman, M Amin Arnaout
1Structural Biology Program, Leukocyte Biology and Inflammation Program, Nephrology Division, Massachusetts General Hospital and Harvard Medical School, Charlestown, USA.
Abstract:
Integrins are large modular cell-surface receptors that regulate almost every aspect of cellular function through bidirectional signals transmitted across the lipid bilayer. Regulation of integrin activity is accomplished by complex and still incompletely understood biochemical pathways that modify integrin ligand binding, clustering, trafficking, and signaling functions. The dynamic tertiary and quaternary changes required to channel some of these activities have hampered, until recently, the crystal structure determination of these heterodimeric receptors. In this chapter, we review the methods used to purify and characterize these proteins biophysically and functionally, and to derive their three-dimensional structures.
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