3DGJ
NNFGAIL segment from Islet Amyloid Polypeptide (IAPP or amylin)
Summary for 3DGJ
| Entry DOI | 10.2210/pdb3dgj/pdb |
| Related | 3DG1 |
| Descriptor | NNFGAIL peptide (2 entities in total) |
| Functional Keywords | iapp, amylin, amyloid, steric zipper, protein fibril |
| Total number of polymer chains | 1 |
| Total formula weight | 747.84 |
| Authors | Wiltzius, J.J.,Sievers, S.A.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. (deposition date: 2008-06-13, release date: 2008-07-01, Last modification date: 2024-02-21) |
| 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: 18556473DOI: 10.1110/ps.036509.108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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