Structural response to mutation at a protein-protein interface

We have crystallised three mutants of the barnase-barstar complex in which interactions across the interface have been deleted by simultaneous mutation of both residues involved in the interaction. Each mutant deletes a different type of interaction at the interface: the first complex bnHis102-->...

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Veröffentlicht in:	Journal of molecular biology 1999-03, Vol.286 (5), p.1487-1506
Hauptverfasser:	Vaughan, C K, Buckle, A M, Fersht, A R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Bacillus - chemistry Bacillus - enzymology Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Crystallization Crystallography, X-Ray Hydrogen Bonding Models, Molecular Mutation Protein Binding Protein Conformation Ribonucleases - chemistry Ribonucleases - genetics Ribonucleases - metabolism Solvents Static Electricity Surface Properties Thermodynamics Water - chemistry Water - metabolism
Online-Zugang:	Volltext
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