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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

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.

Author: Schlessinger, Joseph, Harrison, Stephen C., Hubbard, Stevan R., Mohammadi, Moosa, Eck, Michael J., Eng, Charis, Songyang, Zhou, Carraway, Kermit L., III, Feldman, Ricardo A., Smith, Darrin P.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
Enzymes, Protein tyrosine kinase, Protein-tyrosine kinase, Enzyme structure-activity relationships

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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.

Author: Meng, Wuyi, Eck, Michael J., Burakoff, Steven J., Sawasdikosol, Sansana
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
Analysis, Protein binding, Protein research

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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.

Author: Harrison, Stephen C., Springer, Timothy A., Casasnovas, Jose M., Liu, Jin-huan, Wang, Jia-huai
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
Cell adhesion molecules, Proteins, Protein structure

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Subjects list: Research
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