4bg6

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m (Protected "4bg6" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4bg6| PDB=4bg6 | SCENE= }}
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===14-3-3 interaction with Rnd3 prenyl-phosphorylation motif===
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{{ABSTRACT_PUBMED_23622247}}
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The entry 4bg6 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> [[http://www.uniprot.org/uniprot/RND3_HUMAN RND3_HUMAN]] Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.
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Authors: Riou, P., Kjaer, S., Purkiss, A., O'Reilly, N., McDonald, N.Q.
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==About this Structure==
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[[4bg6]] is a 4 chain structure with sequence 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=4BG6 OCA].
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Description: 14-3-3 interaction with Rnd3 prenyl-phosphorylation motif
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==Reference==
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<ref group="xtra">PMID:023622247</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Kjaer, S.]]
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[[Category: McDonald, N Q.]]
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[[Category: Purkiss, A.]]
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[[Category: Reilly, N O.]]
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[[Category: Riou, P.]]
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[[Category: Actin cytoskeleton]]
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[[Category: Prenylation]]
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[[Category: Signaling protein]]

Revision as of 15:02, 19 June 2013

Template:STRUCTURE 4bg6

Contents

14-3-3 interaction with Rnd3 prenyl-phosphorylation motif

Template:ABSTRACT PUBMED 23622247

Function

[1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.[1] [2] [3] [4] [5] [RND3_HUMAN] Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.

About this Structure

4bg6 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Riou P, Kjaer S, Garg R, Purkiss A, George R, Cain RJ, Bineva G, Reymond N, McColl B, Thompson AJ, O'Reilly N, McDonald NQ, Parker PJ, Ridley AJ. 14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit g proteins. Cell. 2013 Apr 25;153(3):640-53. doi: 10.1016/j.cell.2013.03.044. PMID:23622247 doi:10.1016/j.cell.2013.03.044
  1. ↑ Dubois T, Rommel C, Howell S, Steinhussen U, Soneji Y, Morrice N, Moelling K, Aitken A. 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J Biol Chem. 1997 Nov 14;272(46):28882-8. PMID:9360956
  2. ↑ Zheng W, Zhang Z, Ganguly S, Weller JL, Klein DC, Cole PA. Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation. Nat Struct Biol. 2003 Dec;10(12):1054-7. Epub 2003 Oct 26. PMID:14578935 doi:10.1038/nsb1005
  3. ↑ Tsuruta F, Sunayama J, Mori Y, Hattori S, Shimizu S, Tsujimoto Y, Yoshioka K, Masuyama N, Gotoh Y. JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. EMBO J. 2004 Apr 21;23(8):1889-99. Epub 2004 Apr 8. PMID:15071501 doi:10.1038/sj.emboj.7600194
  4. ↑ Ganguly S, Weller JL, Ho A, Chemineau P, Malpaux B, Klein DC. Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205. Proc Natl Acad Sci U S A. 2005 Jan 25;102(4):1222-7. Epub 2005 Jan 11. PMID:15644438 doi:0406871102
  5. ↑ Gu YM, Jin YH, Choi JK, Baek KH, Yeo CY, Lee KY. Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon. FEBS Lett. 2006 Jan 9;580(1):305-10. Epub 2005 Dec 19. PMID:16376338 doi:S0014-5793(05)01485-7

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