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Iterative Crystallography Service:Mu-crystallin homolog

Iterative Crystallography Service:Mu-crystallin homolog

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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

2I99

MMDB ID

44495

Source

E.coli

Method

X-Ray Diffraction

Resolution

2.6 Å

Ligand Chemical Component

NAD

Gene information

Gene Name

CRYM

Synonyms

DFNA40; THBP; NADP-regulated thyroid-hormone binding protein; OTTHUMP00000115878; dfna40; crystallin mu

UniProt ID

Q14894

GeneID

1428

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