Unusual domain pairing in a mutant of bovine lens γB-crystallin
- 1 June 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 279 (5) , 1053-1059
- https://doi.org/10.1006/jmbi.1998.1850
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- The domains in γb-crystallin: identical fold-different stabilitiesJournal of Molecular Biology, 1997
- Structure of Bovine Eye Lens γD (γIIIb)-Crystallin at 1.95 ÅActa Crystallographica Section D-Biological Crystallography, 1996
- 3D domain swapping: A mechanism for oligomer assemblyProtein Science, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Domain interactions and connecting peptides in lens crystallinsJournal of Molecular Biology, 1994
- Structure of the bovine eye lens protein γB(γII)-crystallin at 1.47 ÅActa Crystallographica Section D-Biological Crystallography, 1993
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteinsNature, 1990
- The evolution of lenticular proteins: The β- and γ-crystallin super gene familyProgress in Biophysics and Molecular Biology, 1988
- Short-range order of crystallin proteins accounts for eye lens transparencyNature, 1983