1csk

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{{STRUCTURE_1csk| PDB=1csk | SCENE= }}
{{STRUCTURE_1csk| PDB=1csk | SCENE= }}
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'''THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP'''
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===THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_7511113}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 7511113 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7511113}}
==About this Structure==
==About this Structure==
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[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:04:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:17:24 2008''

Revision as of 18:17, 30 June 2008

Image:1csk.png

Template:STRUCTURE 1csk

THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP

Template:ABSTRACT PUBMED 7511113

About this Structure

1CSK is a Single protein structure of sequence from Homo sapiens. 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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