4hkc
From Proteopedia
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| - | + | {{STRUCTURE_4hkc| PDB=4hkc | SCENE= }} | |
| + | ===14-3-3-zeta in complex with S1011 phosphorylated integrin alpha-4 peptide=== | ||
| + | {{ABSTRACT_PUBMED_23763993}} | ||
| - | + | ==Function== | |
| + | [[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/ITA4_HUMAN ITA4_HUMAN]] Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. | ||
| - | + | ==About this Structure== | |
| + | [[4hkc]] is a 2 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=4HKC OCA]. | ||
| - | + | ==Reference== | |
| + | <ref group="xtra">PMID:023763993</ref><references group="xtra"/><references/> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Bonet, R.]] | ||
| + | [[Category: Campbell, I D.]] | ||
| + | [[Category: 14-3-3]] | ||
| + | [[Category: All-helical protein]] | ||
| + | [[Category: Alpha-4 integrin tail]] | ||
| + | [[Category: Phosphorylation]] | ||
| + | [[Category: Regulatory]] | ||
| + | [[Category: Signal transduction]] | ||
| + | [[Category: Signaling protein-peptide complex]] | ||
Revision as of 10:14, 30 June 2013
Contents |
14-3-3-zeta in complex with S1011 phosphorylated integrin alpha-4 peptide
Template:ABSTRACT PUBMED 23763993
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] [ITA4_HUMAN] Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells.
About this Structure
4hkc is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Bonet R, Vakonakis I, Campbell ID. Characterization of 14-3-3-zeta Interactions with Integrin Tails. J Mol Biol. 2013 Jun 11. pii: S0022-2836(13)00354-9. doi:, 10.1016/j.jmb.2013.05.024. PMID:23763993 doi:10.1016/j.jmb.2013.05.024
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
