2iyc

From Proteopedia

(Difference between revisions)

Revision as of 07:34, 15 April 2020

SENP1 native structure

Structural highlights

2iyc is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ckg, 2ckh, 2iy0, 2iy1, 2iyd
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SENP1_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gong L, Millas S, Maul GG, Yeh ET. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem. 2000 Feb 4;275(5):3355-9. PMID:10652325
↑ Cheng J, Wang D, Wang Z, Yeh ET. SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol Cell Biol. 2004 Jul;24(13):6021-8. PMID:15199155 doi:10.1128/MCB.24.13.6021-6028.2004
↑ Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y. Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1. FEBS Lett. 2005 Nov 7;579(27):6272-8. Epub 2005 Oct 19. PMID:16253240 doi:S0014-5793(05)01251-2
↑ Shen LN, Dong C, Liu H, Naismith JH, Hay RT. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580 doi:10.1042/BJ20052030
↑ Shen LN, Dong C, Liu H, Naismith JH, Hay RT. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580 doi:10.1042/BJ20052030

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iyc"

@@ Line 1: / Line 1: @@
 ==SENP1 native structure==
-<StructureSection load='2iyc' size='340' side='right' caption='[[2iyc]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
+<StructureSection load='2iyc' size='340' side='right'caption='[[2iyc]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iyc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IYC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iyc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IYC FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ckg|2ckg]], [[2ckh|2ckh]], [[2iy0|2iy0]], [[2iy1|2iy1]], [[2iyd|2iyd]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyc OCA], [http://pdbe.org/2iyc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iyc RCSB], [http://www.ebi.ac.uk/pdbsum/2iyc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyc ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2iyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyc OCA], [http://pdbe.org/2iyc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iyc RCSB], [http://www.ebi.ac.uk/pdbsum/2iyc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyc ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Dong, C]]
 [[Category: Naismith, J H]]

2iyc

From Proteopedia

Revision as of 07:34, 15 April 2020

SENP1 native structure

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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