2bzx

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[[Image:2bzx.gif|left|200px]]<br /><applet load="2bzx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bzx.gif|left|200px]]
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caption="2bzx, resolution 2.8&Aring;" />
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'''ATOMIC MODEL OF CRKL-SH3C MONOMER'''<br />
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{{Structure
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|PDB= 2bzx |SIZE=350|CAPTION= <scene name='initialview01'>2bzx</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''ATOMIC MODEL OF CRKL-SH3C MONOMER'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BZX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZX OCA].
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2BZX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZX OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17161365 17161365]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17161365 17161365]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: sh3c]]
[[Category: sh3c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:57 2008''

Revision as of 14:08, 20 March 2008


PDB ID 2bzx

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, resolution 2.8Å
Coordinates: save as pdb, mmCIF, xml



ATOMIC MODEL OF CRKL-SH3C MONOMER


Overview

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.

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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