Analysis of GTPases carrying hydrophobic amino acid substitutions in lieu of the catalytic glutamine: Implications for GTP hydrolysis

Proteins: Structure, Function and Genetics

Volumn 59, Issue 2, 2005, Pages 332-338

  Mishra, Rajeev ^a   Gara, Sudheer Kumar ^b   Mishra, Shambhavi ^b   Prakash, Balaji ^b  

^a JAWAHARLAL NEHRU UNIVERSITY   (India)

^b INDIAN INSTITUTE OF TECHNOLOGY KANPUR   (India)

Author keywords

Catalytic residues; Conformational change; GTP binding protein; Homology modeling; Hydrophobic stabilization; Transition state

Indexed keywords

ASPARTIC ACID; GLUTAMINE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; PROTEIN HGBP1; PROTEIN YLQF; RAS PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CARCINOGENICITY; CATALYSIS; CRYSTAL STRUCTURE; ENZYME CONFORMATION; HYDROLYSIS; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR MODEL; MOLECULAR STABILITY; MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; SIGNAL TRANSDUCTION;

AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; GLUTAMINE; GTP PHOSPHOHYDROLASES; GTP-BINDING PROTEINS; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; LIGANDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 16344363783     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20413     Document Type: Article

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