2bzx

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[[Image:2bzx.gif|left|200px]]
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{{Seed}}
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[[Image:2bzx.png|left|200px]]
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{{STRUCTURE_2bzx| PDB=2bzx | SCENE= }}
{{STRUCTURE_2bzx| PDB=2bzx | SCENE= }}
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'''ATOMIC MODEL OF CRKL-SH3C MONOMER'''
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===ATOMIC MODEL OF CRKL-SH3C MONOMER===
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==Overview==
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CRKL plays essential roles in cell signaling. It consists of an N-terminal SH2 domain followed by two SH3 domains. SH2 and SH3N bind to signaling proteins, but the function of the SH3C domain has remained largely enigmatic. We show here that the SH3C of CRKL forms homodimers in protein crystals and in solution. Evidence for dimer formation of full-length CRKL is also presented. In the SH3C dimer, a nuclear export signal (NES) is mostly buried under the domain surface. The same is true for a monomeric SH3C obtained under different crystallization conditions. Interestingly, partial SH3 unfolding, such as occurs upon dimer/monomer transition, produces a fully-accessible NES through translocation of a single beta strand. Our results document the existence of an SH3 domain dimer formed through exchange of the first SH3 domain beta strand and suggest that partial unfolding of the SH3C is important for the relay of information in vivo.
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The line below this paragraph, {{ABSTRACT_PUBMED_17161365}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17161365 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17161365}}
==About this Structure==
==About this Structure==
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[[Category: Crkl,sh3c,monomer,native,nuclear export]]
[[Category: Crkl,sh3c,monomer,native,nuclear export]]
[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:02:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:47:27 2008''

Revision as of 17:47, 28 July 2008

Image:2bzx.png

Template:STRUCTURE 2bzx

ATOMIC MODEL OF CRKL-SH3C MONOMER

Template:ABSTRACT PUBMED 17161365

About this Structure

2BZX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal., Harkiolaki M, Gilbert RJ, Jones EY, Feller SM, Structure. 2006 Dec;14(12):1741-53. PMID:17161365

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