Iterative Crystallography Service:Mu-crystallin homolog
产品名称: Iterative Crystallography Service:Mu-crystallin homolog
英文名称: Iterative Crystallography Service:Mu-crystallin homolog
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http://www.creative-biostructure.com/Iterative-crystallography/Iterative-crystallography-CBCRY14.htm
Cat. No. |
CBCRY14 |
|
Background |
Crystallins are separated into two classes: taxon-specific and ubiquitous. The former class is also called phylogenetically-restricted crystallins. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. This gene encodes a taxon-specific crystallin protein that binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. The encoded protein does not perform a structural role in lens tissue, and instead it binds thyroid hormone for possible regulatory or developmental roles. Multiple alternatively spliced transcript variants have been found for this gene. |
|
Molecular description |
Protein Classification |
Oxidoreductase |
Structure Weight |
68589.65 Da |
|
Polymer |
1 |
|
Molecule |
Mu-crystallin homolog |
|
Chain Length |
312 amino acids |
|
Crystal Description |
PDB ID |
|
MMDB ID |
||
Source |
E.coli |
|
Method |
X-Ray Diffraction |
|
Resolution |
2.6 Å |
|
Ligand Chemical Component |
NAD |
|
Gene information |
Gene Name |
|
Synonyms |
DFNA40; THBP; NADP-regulated thyroid-hormone binding protein; OTTHUMP00000115878; dfna40; crystallin mu |
|
UniProt ID |
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GeneID |
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Chromosome Location |
16p13.11-p12.3 |
|
Function |
NADP or NADPH binding; catalytic activity; thyroid hormone binding; transcription corepressor activity |
|
Reference |
Cheng, Z., Sun, L., He, J., Gong, W. (2007) Crystal structure of human {micro}-crystallin complexed with NADPH Protein Sci. 16: 329-335 |