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2i99
From Proteopedia
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{{STRUCTURE_2i99| PDB=2i99 | SCENE= }} | {{STRUCTURE_2i99| PDB=2i99 | SCENE= }} | ||
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===Crystal structure of human Mu_crystallin at 2.6 Angstrom=== | ===Crystal structure of human Mu_crystallin at 2.6 Angstrom=== | ||
| + | {{ABSTRACT_PUBMED_17242435}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/CRYM_HUMAN CRYM_HUMAN]] Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors.<ref>PMID:21332720</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:017242435</ref><references group="xtra"/> | + | <ref group="xtra">PMID:017242435</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Cheng, Z.]] | [[Category: Cheng, Z.]] | ||
Revision as of 08:19, 23 April 2014
Contents |
Crystal structure of human Mu_crystallin at 2.6 Angstrom
Template:ABSTRACT PUBMED 17242435
Function
[CRYM_HUMAN] Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors.[1]
About this Structure
2i99 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Cheng Z, Sun L, He J, Gong W. Crystal structure of human micro-crystallin complexed with NADPH. Protein Sci. 2007 Feb;16(2):329-35. PMID:17242435 doi:http://dx.doi.org/16/2/329
- ↑ Hallen A, Cooper AJ, Jamie JF, Haynes PA, Willows RD. Mammalian forebrain ketimine reductase identified as mu-crystallin; potential regulation by thyroid hormones. J Neurochem. 2011 Aug;118(3):379-87. doi: 10.1111/j.1471-4159.2011.07220.x. Epub , 2011 Mar 15. PMID:21332720 doi:http://dx.doi.org/10.1111/j.1471-4159.2011.07220.x
