2iy1: Difference between revisions

Revision as of 17:44, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2iy1.png

Template:STRUCTURE 2iy1

SENP1 (MUTANT) FULL LENGTH SUMO1SENP1 (MUTANT) FULL LENGTH SUMO1

Template:ABSTRACT PUBMED 17099698

About this StructureAbout this Structure

2IY1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

SUMO protease SENP1 induces isomerization of the scissile peptide bond., Shen L, Tatham MH, Dong C, Zagorska A, Naismith JH, Hay RT, Nat Struct Mol Biol. 2006 Dec;13(12):1069-77. Epub 2006 Nov 12. PMID:17099698

Page seeded by OCA on Sun Jul 27 17:44:54 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2iy1.gif|left|200px]]
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 {{STRUCTURE_2iy1|  PDB=2iy1  |  SCENE=  }}
-'''SENP1 (MUTANT) FULL LENGTH SUMO1'''
+===SENP1 (MUTANT) FULL LENGTH SUMO1===
-==Overview==
+<!--
-Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from modified proteins. To establish the proteolytic mechanism, we determined structures of catalytically inactive SENP1 bound to SUMO-1-modified RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond is kinked at a right angle to the C-terminal tail of SUMO-1 and has the cis configuration of the amide nitrogens. SENP1 preferentially processes SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding and is likely to reflect differences in the ability of SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.
+The line below this paragraph, {{ABSTRACT_PUBMED_17099698}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17099698 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17099698}}
 ==About this Structure==
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 [[Category: Ubiquitin]]
 [[Category: Ubl conjugation pathway]]
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