Mu-crystallin homolog

• Cat.No.: CBCRY14

Specification

• Source: E.coli
• Tag: Non
• 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.
• Protein Classification: Oxidoreductase
• Structure Weight: 68589.65 Da
• Polymer: 1
• Molecule: Mu-crystallin homolog
• Chain Length: 312 amino acids
• PDB ID: 2I99
• MMDB ID: 44495
• Method: X-Ray Diffraction
• Resolution: 2.6Å
• Ligand Chemical Component: NAD
• Reference: Cheng, Z., Sun, L., He, J., Gong, W.(2007) Crystal structure of human {micro}-crystallin complexed with NADPHProtein Sci.16: 329-335

Gene Information

• Gene Name: CRYM
• Synonyms: DFNA40; THBP; NADP-regulated thyroid-hormone binding protein; OTTHUMP00000115878; dfna40; crystallin mu
• UniProt ID: Q14894
• Gene ID: 1428
• Chromosome Location: 16p13.11-p12.3
• Function: NADP or NADPH binding; catalytic activity; thyroid hormone binding; transcription corepressor activity