3HYD
LVEALYL peptide derived from human insulin chain B, residues 11-17
Summary for 3HYD
| Entry DOI | 10.2210/pdb3hyd/pdb |
| Related | 2OMQ |
| Descriptor | Insulin (2 entities in total) |
| Functional Keywords | amyloid-like protofibril, carbohydrate metabolism, cleavage on pair of basic residues, diabetes mellitus, disease mutation, disulfide bond, glucose metabolism, hormone, pharmaceutical, secreted, protein fibril |
| Cellular location | Secreted: P01308 |
| Total number of polymer chains | 1 |
| Total formula weight | 819.99 |
| Authors | Ivanova, M.I.,Sawaya, M.R.,Eisenberg, D. (deposition date: 2009-06-22, release date: 2009-10-06, Last modification date: 2024-04-03) |
| Primary citation | Ivanova, M.I.,Sievers, S.A.,Sawaya, M.R.,Wall, J.S.,Eisenberg, D. Molecular basis for insulin fibril assembly. Proc.Natl.Acad.Sci.USA, 106:18990-18995, 2009 Cited by PubMed Abstract: In the rare medical condition termed injection amyloidosis, extracellular fibrils of insulin are observed. We found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio-dependent manner, suggesting that this segment is central to the cross-beta spine of the insulin fibril. In isolation from the rest of the protein, LVEALYL forms microcrystalline aggregates with fibrillar morphology, the structure of which we determined to 1 A resolution. The LVEALYL segments are stacked into pairs of tightly interdigitated beta-sheets, each pair displaying the dry steric zipper interface typical of amyloid-like fibrils. This structure leads to a model for fibrils of human insulin consistent with electron microscopic, x-ray fiber diffraction, and biochemical studies. PubMed: 19864624DOI: 10.1073/pnas.0910080106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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