4lsc

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'''Unreleased structure'''
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{{STRUCTURE_4lsc| PDB=4lsc | SCENE= }}
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===Isolated SERK1 co-receptor ectodomain at high resolution===
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{{ABSTRACT_PUBMED_23929946}}
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The entry 4lsc is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/SERK1_ARATH SERK1_ARATH]] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway.<ref>PMID:11509554</ref> <ref>PMID:17693538</ref>
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Authors: Santiago, J., Henzler, C., Hothorn, M.
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==About this Structure==
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[[4lsc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LSC OCA].
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Description:
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==Reference==
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<ref group="xtra">PMID:023929946</ref><references group="xtra"/><references/>
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[[Category: Arabidopsis thaliana]]
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[[Category: Henzler, C.]]
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[[Category: Hothorn, M.]]
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[[Category: Santiago, J.]]
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[[Category: Brassinosteroid binding]]
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[[Category: Lrr-domain]]
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[[Category: Membrane co-receptor]]
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[[Category: N-glycosylation]]
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[[Category: Protein binding]]

Revision as of 10:44, 4 September 2013

Template:STRUCTURE 4lsc

Contents

Isolated SERK1 co-receptor ectodomain at high resolution

Template:ABSTRACT PUBMED 23929946

Function

[SERK1_ARATH] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway.[1] [2]

About this Structure

4lsc is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

  • Santiago J, Henzler C, Hothorn M. Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases. Science. 2013 Aug 23;341(6148):889-92. doi: 10.1126/science.1242468. Epub 2013, Aug 8. PMID:23929946 doi:10.1126/science.1242468
  1. Shah K, Vervoort J, de Vries SC. Role of threonines in the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 activation loop in phosphorylation. J Biol Chem. 2001 Nov 2;276(44):41263-9. Epub 2001 Aug 16. PMID:11509554 doi:10.1074/jbc.M102381200
  2. Aker J, Hesselink R, Engel R, Karlova R, Borst JW, Visser AJ, de Vries SC. In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy. Plant Physiol. 2007 Oct;145(2):339-50. Epub 2007 Aug 10. PMID:17693538 doi:10.1104/pp.107.103986

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