Comparison of the low energy conformations of an oncogenic and a non-oncogenic p21 protein, neither of which binds GTP or GDP

Journal of Protein Chemistry

Volumn 13, Issue 2, 1994, Pages 237-251

  Liwo, Adam ^a,b   Gibson, Kenneth D ^b   Scheraga, Harold A ^b   Brandt Rauf, Paul W ^c   Monaco, Regina ^d   Pincus, Matthew R ^a  

^a SUNY UPSTATE MEDICAL UNIVERSITY   (United States)

^b Cornell University ^*  (United States)

^c New York Presbyterian Columbia University Medical Center   (United States)

^d NEW YORK UNIVERSITY   (United States)

Author keywords

binding; Conformation; EDMC; p21 protein

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PROTEIN P21;

AMINO ACID SUBSTITUTION; ARTICLE; CALCULATION; CARCINOGENICITY; CELL TRANSFORMATION; ENERGY CONSUMPTION; ENERGY METABOLISM; MOLECULAR CLONING; PROTEIN BINDING; PROTEIN CONFORMATION;

COMPARATIVE STUDY; CRYSTALLOGRAPHY, X-RAY; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MUTATION; ONCOGENE PROTEIN P21(RAS); PROTEIN CONFORMATION; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0028207563     PISSN: 02778033     EISSN: 15734943     Source Type: Journal    
DOI: 10.1007/BF01891982     Document Type: Article

References (43)

1. The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR
2. Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids
3. Standard-geometry chains fitted to X-ray derived structures: Validation of the rigid-geometry approximation. I. Chain closure through a limited search of ?loop? conformations