2mau | pdb_00002mau

Solution structure of alpha-amylase inhibitor wrightide R1 (wR1) peptide from Wrightia religiosa

spinqualitylabelsall models 2mau Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mau is a 1 chain structure with sequence from Wrightia religiosa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 10 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function V5W9K8_9GENT Publication Abstract from PubMed Obesity and type-2 diabetes are chronic metabolic diseases that could be benefited by the use of alpha-amylase inhibitors to manage starch intake. The pseudocyclics, wrightides Wr-AI1 to Wr-AI3, isolated from an Apocynaceae plant show promising potentials for further development as orally active alpha-amylase inhibitors. These linear peptides retain the stability known for cystine knot peptides in harsh treatment. They are resistant to treatment by heat, endopeptidase or exopeptidase, characteristics of cyclic cystine knot peptides. Our NMR and crystallography analysis also showed that wrightides, currently the smallest proteinaceous alpha -amylase inhibitors reported, contain the backbone-twisting cis proline which is preceded by a non-aromatic residue rather than a conventional aromatic residue. Modeled structure and molecular dynamics study of Wr-AI1 in complex with yellow meal worm alpha-amylase suggested that despite similar structure and cystine knot fold, members of knottin-type alpha-amylase inhibitors may bind to insect alpha-amylase via a different set of interactions. Finally, we showed that the precursors of pseudocyclic cystine knot alpha-amylase inhibitors and their biosynthesis in plants follow secretory protein synthesis pathway. Together, our work provides insights for the use of the pseudocyclic alpha-amylase inhibitors as useful leads for developing orally active peptidyl bioactives as well as an alternative scaffold to cyclic peptides for engineering metabolic-stable human alpha-amylase inhibitors. This article is protected by copyright. All rights reserved. Discovery and Characterization of Pseudocyclic Cystine-Knot alpha-Amylase Inhibitors with High Resistance to Heat and Proteolytic Degradation.,Nguyen PQ, Wang S, Kumar A, Yap LJ, Luu TT, Lescar J, Tam JP FEBS J. 2014 Jul 21. doi: 10.1111/febs.12939. PMID:25040200 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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