Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain

Molecular and Cellular Biochemistry

Volumn 158, Issue 1, 1979, Pages 57-63

  Xu, Bin ^a   Miller, W Todd ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

protein folding; SH2 domain; SH3 domain; tyrosine kinase; v Src

Indexed keywords

GUANIDINE; HYBRID PROTEIN; PROTEIN TYROSINE KINASE; SYNTHETIC PEPTIDE;

ARTICLE; AUTOPHOSPHORYLATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME PHOSPHORYLATION; ENZYME STABILITY; ENZYME SUBSTRATE; EXPRESSION VECTOR; NONHUMAN; ONCOGENE SRC; PROTEIN DOMAIN; PROTEIN EXPRESSION; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ESCHERICHIA COLI; GLUTATHIONE TRANSFERASE; MOLECULAR SEQUENCE DATA; ONCOGENE PROTEIN PP60(V-SRC); ONCOGENE PROTEINS V-ABL; PEPTIDES; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN-TYROSINE KINASES; RECOMBINANT FUSION PROTEINS; SRC HOMOLOGY DOMAINS;

EID: 0029936233     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/BF00225883     Document Type: Article

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