2KIB
Protein Fibril
Summary for 2KIB
| Entry DOI | 10.2210/pdb2kib/pdb |
| Related | 2g48 3dgj |
| NMR Information | BMRB: 20074 |
| Descriptor | NFGAIL segment from human islet amyloid polypeptide (1 entity in total) |
| Functional Keywords | protein fibril, iapp, amylin, snnfgailss, symmetry |
| Total number of polymer chains | 8 |
| Total formula weight | 5766.52 |
| Authors | Nielsen, J.T.,Bjerring, M.,Jeppesen, M.D.,Pedersen, R.O.,Pedersen, J.M.,Hein, K.L.,Vosegaard, T.,Skrydstrup, T.,Otzen, D.E.,Nielsen, N. (deposition date: 2009-05-01, release date: 2009-09-08, Last modification date: 2024-05-01) |
| Primary citation | Nielsen, J.T.,Bjerring, M.,Jeppesen, M.D.,Pedersen, R.O.,Pedersen, J.M.,Hein, K.L.,Vosegaard, T.,Skrydstrup, T.,Otzen, D.E.,Nielsen, N.C. Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy. Angew.Chem.Int.Ed.Engl., 48:2118-2121, 2009 Cited by PubMed Abstract: The fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 A resolution. Symmetry information contained in the easily obtainable resonance assignments from solid-state NMR spectra (see picture), along with long-range constraints, can be applied to uniquely identify the supramolecular organization of fibrils. PubMed: 19130518DOI: 10.1002/anie.200804198 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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