Comparison of molecular dynamics averaged structures for complexes of normal and oncogenic ras-p21 with SOS nucleotide exchange protein, containing computed conformations for three crystallographically undefined domains, suggests a potential role of these domains in ras signaling

Protein Journal

Volumn 23, Issue 3, 2004, Pages 217-228

  Duncan, Thomas ^a   Chen, James M ^b   Friedman, Fred K ^c   Hyde, Mark ^d   Chie, Lyndon ^f   Pincus, Matthew R ^e,f  

^a SUNY UPSTATE MEDICAL UNIVERSITY   (United States)

^b GILEAD SCIENCES   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

^d Advanced Computing Services   (United States)

^e VETERANS AFFAIRS MEDICAL CENTER   (United States)

^f SUNY Downstate Medical Center   (United States)

Author keywords

Average structure; Effector domains; Molecular dynamics; Oncogenic ras 21; SOS loop regions; SOS protein; Wild type ras p21

Indexed keywords

ANTIPORTER; BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; PROTEIN P21; RAS PROTEIN; SOS PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTALLOGRAPHY; MOLECULAR DYNAMICS; NONHUMAN; ONCOGENE RAS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; ANIMAL; BINDING SITE; CHEMISTRY; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

ANIMALS; BINDING SITES; HUMANS; ONCOGENE PROTEIN P21(RAS); PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; SON OF SEVENLESS PROTEINS;

EID: 16544395812     PISSN: 15723887     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JOPC.0000026417.72621.1f     Document Type: Article

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