Catalytic specificity of protein-tyrosine kinases is critical for selective signalling
Article Abstract:
An analysis of several protein-tyrosine kinases suggests that the specificity of these kinases arises due to the ability of the SH2 domains to identify phosphotyrosine. The receptor tyrosine kinases phosphorylate group III SH2 domain-recognized peptides, while those recognized by group I SH2 domains are phosphorylated by cytosolic tyrosine kinases. Any mutation on the tyrosine kinases results in a variation in peptide substrate specificity, corroborating the need for catalytic specificity for selective signaling in human diseases.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
Article Abstract:
The three-dimensional structure of Cbl-N, the evolutionarily conserved amino-terminal region of the adaptor protein Cbl, has been determined in order to improve understanding of its diverse recognition and regulatory functions. It has been established that Cbl-N is made up of an N-terminal four-helix bundle, a calcium-binding domain with the EF-hand fold and an SH2 domain. It appears that these three domains together form an integrated structure that is vital for phosphoprotein recognition.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface
Article Abstract:
The crystal structure of the intercellular adhesion molecule ICAM-2's extracellular region is presented. In this structure, the aspartic acid residue and fibronectin lie in protruding loops while glutamic acid residue, which is surrounded by a flat recognition surface, lies on a beta-strand. This may indicate variances in the structure of recognition sites between integrins that lack or contain I domains.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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