Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly

Protein Science : a Publication of the Protein Society
G WrightC Slingsby

Abstract

The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.

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Citations

Aug 11, 2004·Progress in Biophysics and Molecular Biology·Hans BloemendalAnnette Tardieu
Mar 26, 2003·Protein Expression and Purification·M K Jobby, Yogendra Sharma
Jan 11, 2000·Eye·C Slingsby, N J Clout
Jun 27, 2002·European Journal of Biochemistry·Giuseppe D'Alessio
May 10, 2001·Protein Science : a Publication of the Protein Society·X Ni, H K Schachman
Nov 17, 2007·BMC Structural Biology·Alexej Abyzov, Valentin A Ilyin
Mar 7, 2014·Progress in Biophysics and Molecular Biology·Amita MishraYogendra Sharma
Jun 7, 2014·Scientific Reports·K MahendiranB K Pierscionek
Feb 8, 2013·Protein Science : a Publication of the Protein Society·Christine SlingsbyAlice R Clark
Nov 23, 2010·Trends in Biotechnology·Ying Yu, Stefan Lutz
Mar 2, 2010·Experimental Eye Research·Magalie MichielStéphanie Finet
Oct 24, 2003·Protein Science : a Publication of the Protein Society·Rob L M Van MontfortChristine Slingsby
Oct 27, 2007·Protein Science : a Publication of the Protein Society·Jannette CareySara Linse
Jan 5, 2005·Nature Reviews. Genetics·Oren S Harman
Nov 19, 2020·Physical Chemistry Chemical Physics : PCCP·José-Luis Velasco-Bolom, Laura Domínguez

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