3dg1 | pdb_00003dg1

Segment SSTNVG derived from IAPP

spinqualitylabelsall models 3dg1, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dg1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function IAPP_HUMAN Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. Publication Abstract from PubMed Human Islet Amyloid Polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG were determined and form the basis of a model for the most commonly observed, full-length IAPP polymorph. Atomic structure of the cross-{beta} spine of Islet Amyloid Polypeptide (Amylin).,Wiltzius JJ, Sievers SA, Sawaya MR, Cascio D, Popov D, Riekel C, Eisenberg D Protein Sci. 2008 Jun 12;. PMID:18556473 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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