Literature DB >> 12136155

Crystallization and preliminary crystallographic analysis of the ezrin FERM domain.

William J Smith1, Richard A Cerione.   

Abstract

Ezrin is a member of the ERM (ezrin/radixin/moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and that also function, both upstream and downstream of the small G-protein Rho, in signaling cascades that regulate the assembly of actin stress fibers. In this study, crystals were obtained of the amino-terminal 297 residues (referred to as FERM) of ezrin. The crystals of the FERM domain of ezrin belong to the monoclinic space group P2(1), with unit-cell parameters a = 48.5, b = 112.8, c = 66.3 A, beta = 102.3 degrees, and contain two molecules in the asymmetric unit. A 2.3 A data set was collected using synchrotron radiation at CHESS A1.

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Year:  2002        PMID: 12136155     DOI: 10.1107/s0907444902010004

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  4 in total

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Journal:  J Proteome Res       Date:  2013-12-17       Impact factor: 4.466

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Journal:  Mol Biol Cell       Date:  2006-03-15       Impact factor: 4.138

3.  Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1.

Authors:  Sophie Béraud-Dufour; Romain Gautier; Corinne Albiges-Rizo; Pierre Chardin; Eva Faurobert
Journal:  FEBS J       Date:  2007-10-03       Impact factor: 5.542

4.  Characterization of the Ca2+ -regulated ezrin-S100P interaction and its role in tumor cell migration.

Authors:  Judith Austermann; Ali Reza Nazmi; Carsten Müller-Tidow; Volker Gerke
Journal:  J Biol Chem       Date:  2008-08-25       Impact factor: 5.157

  4 in total

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