1ayo | pdb_00001ayo
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RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN
Overview
BACKGROUND: The large plasma proteinase inhibitors of the alpha, 2-macroglobulin superfamily inhibit proteinases by capturing them within a, central cavity of the inhibitor molecule. After reaction with the, proteinase, the alpha-macroglobulin-proteinase complex binds to the, alpha-macroglobulin receptor, present in the liver and other tissues, and, becomes endocytosed and rapidly removed from the circulation. The complex, binds to the receptor via recognition sites located on a separate domain, of approximately 138 residues positioned at the C terminus of the, alpha-macroglobulin subunit. RESULTS: The crystal structure of the, receptor-binding domain of bovine alpha 2-macroglobulin (bRBD) has been, determined at a resolution of 1.9 A. The domain primarily comprises a, nine-strand beta structure with a jelly-roll topology, but also contains, two small alpha helices. CONCLUSIONS: The surface patch responsible for, receptor recognition is thought to involve residues located on one of the, two alpha helices of the bRBD as well as residues in two of the beta, strands. Located on this alpha helix are two lysine residues that are, important for receptor binding. The structure of bRBD is very similar to, the approximately 100-residue C-terminal domain of factor XIII, a, transglutaminase from the blood coagulation system.
Disease
Known diseases associated with this structure: Alzheimer disease, susceptibility to OMIM:[103950], Emphysema due to alpha-2-macroglobulin deficiency OMIM:[103950]
About this Structure
1AYO is a Single protein structure of sequence from Bos taurus with CA as ligand. Known structural/functional Sites: S1 and S2. Full crystallographic information is available from OCA.
Reference
Crystal structure of the receptor-binding domain of alpha 2-macroglobulin., Jenner L, Husted L, Thirup S, Sottrup-Jensen L, Nyborg J, Structure. 1998 May 15;6(5):595-604. PMID:9634697
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