4hvw

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{{STRUCTURE_4hvw| PDB=4hvw | SCENE= }}
{{STRUCTURE_4hvw| PDB=4hvw | SCENE= }}
===Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide VSL12===
===Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide VSL12===
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{{ABSTRACT_PUBMED_23633584}}
==Function==
==Function==
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==Reference==
==Reference==
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<references group="xtra"/><references/>
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<ref group="xtra">PMID:023633584</ref><references group="xtra"/><references/>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Non-specific protein-tyrosine kinase]]
[[Category: Non-specific protein-tyrosine kinase]]

Revision as of 15:11, 19 June 2013

Template:STRUCTURE 4hvw

Contents

Crystal structure of the T98E c-Src-SH3 domain mutant in complex with the high affinity peptide VSL12

Template:ABSTRACT PUBMED 23633584

Function

[SRC_CHICK] Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra-cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus.[1] [2]

About this Structure

4hvw is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

  • Bacarizo J, Camara-Artigas A. Atomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and II. Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):756-66. doi:, 10.1107/S0907444913001522. Epub 2013 Apr 11. PMID:23633584 doi:10.1107/S0907444913001522
  1. Kremer NE, D'Arcangelo G, Thomas SM, DeMarco M, Brugge JS, Halegoua S. Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions. J Cell Biol. 1991 Nov;115(3):809-19. PMID:1717492
  2. Simonson MS, Wang Y, Herman WH. Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases. J Biol Chem. 1996 Jan 5;271(1):77-82. PMID:8550628

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