X-ray structures of three interface mutants of gammaB-crystallin from bovine eye lens

Protein Science : a Publication of the Protein Society
S PalmeC Slingsby

Abstract

GammaB-crystallin consists of two domains each comprising two "Greek key" motifs. Both domains fold independently, and domain interactions contribute significantly to the stability of the C-terminal domain. In a previous study (Palme S et al., 1996, Protein Sci 6:1529-1636) it was shown that Phe56 from the N-terminal domain, a residue involved in forming a hydrophobic core at the domain interface, effects the interaction of the two domains, and therefore, the stability of the C-terminal domain. Ala or Asp at position 56 drastically decreased the stability of the C-terminal domain, whereas Trp had a more moderate effect. In this article we present the X-ray structures of these interface mutants and correlate them with the stability data. The mutations do not effect the overall structure of the molecule. No structural changes are observed in the vicinity of the replaced residue, suggesting that the local structure is too rigid to allow compensations for the amino acid replacements. In the mutants gammaB-F56A and -F56D, a solvent-filled groove accessible to the bulk solvent is created by the replacement of the bulky Phe side chain. In gammaB-F56W, the pyrrole moiety of the indole ring replaces the phenyl side chain of the wild typ...Continue Reading

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Citations

Aug 11, 2004·Progress in Biophysics and Molecular Biology·Hans BloemendalAnnette Tardieu
Mar 31, 1999·Progress in Biophysics and Molecular Biology·R Jaenicke
Jan 11, 2000·Eye·C Slingsby, N J Clout
May 20, 2014·Progress in Biophysics and Molecular Biology·Eugene Serebryany, Jonathan A King
Oct 2, 2007·Protein Science : a Publication of the Protein Society·Ishara A MillsJonathan A King
Nov 14, 2001·The Journal of Biological Chemistry·Andrew G PurkissChristine Slingsby
Jun 27, 1998·Journal of Molecular Biology·S PalmeC Slingsby

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