2ckg

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[[Image:2ckg.gif|left|200px]]<br /><applet load="2ckg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ckg.gif|left|200px]]
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caption="2ckg, resolution 2.45&Aring;" />
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'''THE STRUCTURE OF SENP1 SUMO-2 CO-COMPLEX SUGGESTS A STRUCTURAL BASIS FOR DISCRIMINATION BETWEEN SUMO PARALOGUES DURING PROCESSING'''<br />
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{{Structure
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|PDB= 2ckg |SIZE=350|CAPTION= <scene name='initialview01'>2ckg</scene>, resolution 2.45&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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'''THE STRUCTURE OF SENP1 SUMO-2 CO-COMPLEX SUGGESTS A STRUCTURAL BASIS FOR DISCRIMINATION BETWEEN SUMO PARALOGUES DURING PROCESSING'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CKG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 2BZP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKG OCA].
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2CKG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 2BZP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKG OCA].
==Reference==
==Reference==
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The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing., Shen LN, Dong C, Liu H, Naismith JH, Hay RT, Biochem J. 2006 Jul 15;397(2):279-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16553580 16553580]
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The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing., Shen LN, Dong C, Liu H, Naismith JH, Hay RT, Biochem J. 2006 Jul 15;397(2):279-88. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16553580 16553580]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ubl conjugation pathway]]
[[Category: ubl conjugation pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:29 2008''

Revision as of 14:16, 20 March 2008


PDB ID 2ckg

Drag the structure with the mouse to rotate
, resolution 2.45Å
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF SENP1 SUMO-2 CO-COMPLEX SUGGESTS A STRUCTURAL BASIS FOR DISCRIMINATION BETWEEN SUMO PARALOGUES DURING PROCESSING


Overview

The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity.

About this Structure

2CKG is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2BZP. Full crystallographic information is available from OCA.

Reference

The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing., Shen LN, Dong C, Liu H, Naismith JH, Hay RT, Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580

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