1csk
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(New page: 200px<br /> <applet load="1csk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1csk, resolution 2.5Å" /> '''THE CRYSTAL STRUCTUR...)
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Revision as of 14:18, 12 November 2007
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THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP
Overview
SH3 domains are modules occurring in diverse proteins, ranging from, cytoskeletal proteins to signaling proteins, such as tyrosine kinases. The, crystal structure of the SH3 domain of Csk (c-Src specific tyrosine, kinase) has been refined at a resolution of 2.5 A, with an R-factor of, 22.4%. The structure is very similar to the FynSH3 crystal structure. When, comparing CskSH3 and FynSH3 it is seen that the structural and charge, differences of the RT-Src loop and the n-Src loop, near the conserved, Trp47, correlate with different binding properties of these SH3 domains., The structure comparison suggests that those glycines and acid residues, which are very well conserved in the SH3 sequences are important for the, stability of the SH3 fold.
About this Structure
1CSK is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop., Borchert TV, Mathieu M, Zeelen JP, Courtneidge SA, Wierenga RK, FEBS Lett. 1994 Mar 14;341(1):79-85. PMID:7511113
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