NDLI: Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A.

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Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A.

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Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Karplus, P. A. Scheraga, H. A. Pearson, M. A. Dodge, R. W. Laity, J. H.
Description	Country affiliation: United States Author Affiliation: Pearson MA ( Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853-1301, USA.)
Abstract	The Tyr92-Pro93 peptide group of bovine pancreatic ribonuclease A (RNase A) exists in the cis conformation in the native state. From unfolding/refolding kinetic studies of the disulfide-intact wild-type protein and of a variant in which Pro93 had been replaced by Ala, it had been suggested that the Tyr92-Ala93 peptide group also exists in the cis conformation in the native state. Here, we report the crystal structure of the P93A variant. Although there is disorder in the region of residues 92 and 93, the best structural model contains a cis peptide at this position, lending support to the results of the kinetics experiments. We also report the crystal structure of the C[40, 95]A variant, which is an analog of the major rate-determining three-disulfide intermediate in the oxidative folding of RNase A, missing the 40-95 disulfide bond. As had been detected by NMR spectroscopy, the crystal structure of this analog shows disorder in the region surrounding the missing disulfide. However, the global chain fold of the remainder of the protein, including the disulfide bond between Cys65 and Cys72, appears to be unaffected by the mutation.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	7
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1998-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Pancreas Enzymology Protein Folding Ribonuclease, Pancreatic Metabolism Animals Crystallography, X-ray Kinetics Magnetic Resonance Spectroscopy Mutation Protein Conformation Chemistry Genetics Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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