The noncatalytic domains of Lck regulate its dephosphorylation by CD45

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1650, Issue 1-2, 2003, Pages 40-49

  Lefebvre, Dennis C ^a   Felberg, Jackie ^a,b   Cross, Jennifer L ^a   Johnson, Pauline ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b Response Biomedical Corp   (Canada)

Author keywords

CD45; Lck; Protein tyrosine phosphatase; Tyrosine kinase

Indexed keywords

CD45 ANTIGEN; PHOSPHOTYROSINE; PROTEIN KINASE LCK; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN FUNCTION; REGULATORY MECHANISM; ALLOSTERISM; ANIMAL; BINDING SITE; METABOLISM; MOUSE; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; ANIMALS; ANTIGENS, CD45; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); MICE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 0141907307     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00190-0     Document Type: Article

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