3DG1

Segment SSTNVG derived from IAPP

Summary for 3DG1

Entry DOI	10.2210/pdb3dg1/pdb
Related	1YJO 2OMM
Descriptor	SSTNVG from Islet Amyloid Polypeptide (2 entities in total)
Functional Keywords	steric zipper, iapp, sstnvg, amyloid, protein fibril
Total number of polymer chains	1
Total formula weight	563.56
Authors	Wiltzius, J.J.,Sievers, S.A.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. (deposition date: 2008-06-12, release date: 2008-07-01, Last modification date: 2024-04-03)
Primary citation	Wiltzius, J.J.,Sievers, S.A.,Sawaya, M.R.,Cascio, D.,Popov, D.,Riekel, C.,Eisenberg, D. Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin). Protein Sci., 17:1467-1474, 2008 Cited by PubMed Abstract: 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. PubMed: 18556473 DOI: 10.1110/ps.036509.108 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.66 Å)

Structure validation