Tissue inhibitor of metalloproteinases-like, OB-fold
IPR008993
Definition
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 PMID:2793861. 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 PMID:7918391. 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.
24 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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