Protein Domain : Tissue inhibitor of metalloproteinases-like, OB-fold IPR008993

Type	Homologous_superfamily
Description	Tissue inhibitors of metalloproteinases (TIMP) are a family of proteins that can form complexes with extracellular matrix metalloproteinases (such as collagenases) and irreversibly inactivate them [ ]. TIMP and related proteins contains a five-stranded antiparallel β-sheet that is rolled over on itself to form a closed β-barrel, and two short helices, which pack close to one another on the same barrel face. A comparison of the delta TIMP-2 structure with other known protein folds reveals that the β-barrel topology is homologous to that seen in proteins of the oligosaccharide/oligonucleotide binding (OB) fold family, a five-stranded β-sheet coiled to form a closed β-barrel capped by an α-helix located between the third and fourth strands [].Other proteins contain domains with a similar OB-like fold:Netrin-like domain (NTR/C345C module), found in procollagen c-proteinase enhancer protein PCOLCE, and in the complement C5 domain.Laminin-binding domain, found in agrin.
Short Name	TIMP-like_OB-fold