WebApr 7, 2024 · To determine precisely which region of UBXN7 interacts with the RING domain of RNF111, we generated UBXN7 deletion mutants for the UBA, UIM, and UBX domains known to interact respectively with ubiquitin, neddylated cullins, and p97/VCP, and for the UAS domain, a thioredoxin-like fold domain that had so far no assigned function (Fig. 2a). … WebOct 23, 2009 · The classic thioredoxin superfamily (as distinguished from the thioredoxin fold class) represents the largest contribution to the sequence diversity of the whole fold …
TXN thioredoxin [Homo sapiens (human)] - Gene - NCBI
WebJun 1, 2003 · Sequence homology between members is poor, their relatedness lying in the structural similarity of the thioredoxin-like fold (12). It has been proposed that different … WebThioredoxin is a class of small redox proteins known to be present in all organisms. It plays a role in many important ... Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold. The active site contains a dithiols in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce ... community medical center watervliet mi
Thioredoxin —a fold for all reasons - ScienceDirect
WebNov 1, 2006 · The thioredoxin-like fold is found in numerous proteins in. the model genetic organism E. coli and in other species. This particular fold is seen in predominantly redox active. WebBy analogy to human protein disulfide isomerase, SelM and Sep15 are composed of one catalytic a-domain that assumes a thioredoxin-like fold composed of a mixed four-stranded β-sheet and three interspersed α … Thioredoxin is a 12-kD oxidoreductase protein. Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold. The active site contains a dithiols in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce other proteins. For Trx1, this process begins by attack of Cys32, one of the residues conserve… Thioredoxin is a 12-kD oxidoreductase protein. Thioredoxin proteins also have a characteristic tertiary structure termed the thioredoxin fold. The active site contains a dithiols in a CXXC motif. These two cysteines are the key to the ability of thioredoxin to reduce other proteins. For Trx1, this process begins by attack of Cys32, one of the residues conserve… easy sweet and sour pork recipe