3l6r
From Proteopedia
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{{STRUCTURE_3l6r| PDB=3l6r | SCENE= }} | {{STRUCTURE_3l6r| PDB=3l6r | SCENE= }} | ||
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===The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding=== | ===The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding=== | ||
+ | {{ABSTRACT_PUBMED_20106978}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/SRR_HUMAN SRR_HUMAN]] Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.<ref>PMID:11054547</ref> <ref>PMID:20106978</ref> | |
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==About this Structure== | ==About this Structure== | ||
- | + | [[3l6r]] is a 1 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=3L6R OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020106978</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Serine racemase]] | [[Category: Serine racemase]] | ||
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[[Category: Pyridoxal phosphate]] | [[Category: Pyridoxal phosphate]] | ||
[[Category: Serine racemase]] | [[Category: Serine racemase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:35:14 2010'' |
Revision as of 20:17, 4 April 2013
Contents |
The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding
Template:ABSTRACT PUBMED 20106978
Function
[SRR_HUMAN] Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.[1] [2]
About this Structure
3l6r is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J. The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem. 2010 Apr 23;285(17):12873-81. Epub 2010 Jan 27. PMID:20106978 doi:10.1074/jbc.M109.050062
- ↑ De Miranda J, Santoro A, Engelender S, Wolosker H. Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000 Oct 3;256(1-2):183-8. PMID:11054547
- ↑ Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J. The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem. 2010 Apr 23;285(17):12873-81. Epub 2010 Jan 27. PMID:20106978 doi:10.1074/jbc.M109.050062