2io2

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[[Image:2io2.gif|left|200px]]<br /><applet load="2io2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2io2.gif|left|200px]]
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caption="2io2, resolution 2.900&Aring;" />
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'''Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1'''<br />
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{{Structure
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|PDB= 2io2 |SIZE=350|CAPTION= <scene name='initialview01'>2io2</scene>, resolution 2.900&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= SENP2, KIAA1331 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), SUMO1, SMT3C, SMT3H3, UBL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RANGAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IO2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2IO2 OCA].
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2IO2 is a [[Protein complex]] structure of sequences 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=2IO2 OCA].
==Reference==
==Reference==
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Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates., Reverter D, Lima CD, Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. Epub 2006 Nov 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17099700 17099700]
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Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates., Reverter D, Lima CD, Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. Epub 2006 Nov 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17099700 17099700]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ulp]]
[[Category: ulp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:31:42 2008''

Revision as of 15:31, 20 March 2008


PDB ID 2io2

Drag the structure with the mouse to rotate
, resolution 2.900Å
Gene: SENP2, KIAA1331 (Homo sapiens), SUMO1, SMT3C, SMT3H3, UBL1 (Homo sapiens), RANGAP1 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1


Contents

Overview

SUMO processing and deconjugation are essential proteolytic activities for nuclear metabolism and cell-cycle progression in yeast and higher eukaryotes. To elucidate the mechanisms used during substrate lysine deconjugation, SUMO isoform processing and SUMO isoform interactions, X-ray structures were determined for a catalytically inert SENP2 protease domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in complex with SUMO-2 or SUMO-3 precursors. Common features within the active site include a 90 degrees kink proximal to the scissile bond that forces C-terminal amino acid residues or the lysine side chain toward a protease surface that appears optimized for lysine deconjugation. Analysis of this surface reveals SENP2 residues, particularly Met497, that mediate, and in some instances reverse, in vitro substrate specificity. Mutational analysis and biochemistry provide a mechanism for SENP2 substrate preferences that explains why SENP2 catalyzes SUMO deconjugation more efficiently than processing.

Disease

Known diseases associated with this structure: Blood group, Cad system OMIM:[111730], Blood group, Sd system OMIM:[111730], Orofacial cleft 10 OMIM:[601912]

About this Structure

2IO2 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates., Reverter D, Lima CD, Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. Epub 2006 Nov 12. PMID:17099700

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