4l3o

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'''Unreleased structure'''
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{{STRUCTURE_4l3o| PDB=4l3o | SCENE= }}
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===Crystal Structure of SIRT2 in complex with the macrocyclic peptide S2iL5===
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{{ABSTRACT_PUBMED_24389023}}
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The entry 4l3o is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN]] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref>
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Authors: Yamagata, K., Nishimasu, H., Ishitani, R., Nureki, O.
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==About this Structure==
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[[4l3o]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L3O OCA].
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Description: Human protein
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==Reference==
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<ref group="xtra">PMID:024389023</ref><references group="xtra"/><references/>
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[[Category: Ishitani, R.]]
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[[Category: Nishimasu, H.]]
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[[Category: Nureki, O.]]
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[[Category: Yamagata, K.]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Macrocyclic peptide]]
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[[Category: Structural change]]

Revision as of 17:17, 19 February 2014

Template:STRUCTURE 4l3o

Contents

Crystal Structure of SIRT2 in complex with the macrocyclic peptide S2iL5

Template:ABSTRACT PUBMED 24389023

Function

[SIR2_HUMAN] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.[1] [2] [3] [4]

About this Structure

4l3o is a 8 chain structure. Full crystallographic information is available from OCA.

Reference

  • Yamagata K, Goto Y, Nishimasu H, Morimoto J, Ishitani R, Dohmae N, Takeda N, Nagai R, Komuro I, Suga H, Nureki O. Structural Basis for Potent Inhibition of SIRT2 Deacetylase by a Macrocyclic Peptide Inducing Dynamic Structural Change. Structure. 2014 Feb 4;22(2):345-52. doi: 10.1016/j.str.2013.12.001. Epub 2014 Jan, 2. PMID:24389023 doi:http://dx.doi.org/10.1016/j.str.2013.12.001
  1. ↑ North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003 Feb;11(2):437-44. PMID:12620231
  2. ↑ Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol. 2003 May;23(9):3173-85. PMID:12697818
  3. ↑ Rothgiesser KM, Erener S, Waibel S, Luscher B, Hottiger MO. SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310. J Cell Sci. 2010 Dec 15;123(Pt 24):4251-8. doi: 10.1242/jcs.073783. Epub 2010 Nov, 16. PMID:21081649 doi:10.1242/jcs.073783
  4. ↑ Jiang W, Wang S, Xiao M, Lin Y, Zhou L, Lei Q, Xiong Y, Guan KL, Zhao S. Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol Cell. 2011 Jul 8;43(1):33-44. doi: 10.1016/j.molcel.2011.04.028. PMID:21726808 doi:10.1016/j.molcel.2011.04.028

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