TY - JOUR
T1 - Structures of SH2 and SH3 domains. Current opinion in structural biology 1993, 3:828-837
AU - Kuriyan, John
AU - Cowburn, David
PY - 1993
Y1 - 1993
N2 - SH2 and SH3 domains are small protein modules of about 100 and 60 amino acids, respectively, that are found in many proteins involved in intracellular signal transduction. SH2 and SH3 domains mediate protein-protein interactions and modulate enzyme activity by their ability to bind to specific phosphorylated tyrosine residues or proline-rich sequences, respectively. The recent determination of the three-dimensional structures of several SH2 and SH3 domains has led to considerable progress in understanding their mechanism of action, and these structures are the focus of this review.
AB - SH2 and SH3 domains are small protein modules of about 100 and 60 amino acids, respectively, that are found in many proteins involved in intracellular signal transduction. SH2 and SH3 domains mediate protein-protein interactions and modulate enzyme activity by their ability to bind to specific phosphorylated tyrosine residues or proline-rich sequences, respectively. The recent determination of the three-dimensional structures of several SH2 and SH3 domains has led to considerable progress in understanding their mechanism of action, and these structures are the focus of this review.
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U2 - 10.1016/0959-440X(93)90145-B
DO - 10.1016/0959-440X(93)90145-B
M3 - Article
AN - SCOPUS:0027141001
SN - 0959-440X
VL - 3
SP - 828
EP - 837
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 6
ER -