2CEU
Despentapeptide insulin in acetic acid (pH 2)
Summary for 2CEU
| Entry DOI | 10.2210/pdb2ceu/pdb |
| Related | 1A7F 1AI0 1AIY 1B9E 1BEN 1EFE 1EV3 1EV6 1EVR 1FU2 1FUB 1G7A 1G7B 1GUJ 1HIQ 1HIS 1HIT 1HLS 1HTV 1HUI 1IOG 1IOH 1J73 1JCA 1JCO 1K3M 1KMF 1LKQ 1LNP 1LPH 1MHI 1MHJ 1MSO 1OS3 1OS4 1Q4V 1QIY 1QIZ 1QJ0 1RWE 1SF1 1SJT 1SJU 1T0C 1T1K 1T1P 1T1Q 1TRZ 1TYL 1TYM 1UZ9 1VKT 1W8P 1XDA 1XGL 1XW7 1ZEG 1ZEH 1ZNJ 2AIY 2C8Q 2C8R 2HIU 3AIY 4AIY 5AIY |
| Descriptor | INSULIN, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | insulin, despentapeptide, acetic acid, ph 2, carbohydrate metabolism, diabetes mellitus, disease mutation, glucose metabolism, hormone, pharmaceutical |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Secreted: P01308 P01308 |
| Total number of polymer chains | 4 |
| Total formula weight | 10740.14 |
| Authors | Whittingham, J.L.,Zhang, Y.,Zakova, L.,Dodson, E.J.,Turkenburg, J.P.,Brange, J.,Dodson, G.G. (deposition date: 2006-02-10, release date: 2006-03-03, Last modification date: 2024-11-20) |
| Primary citation | Whittingham, J.L.,Youshang, Z.,Zakova, L.,Dodson, E.J.,Turkenburg, J.P.,Brange, J.,Dodson, G.G. I222 Crystal Form of Despentapeptide (B26-B30) Insulin Provides New Insights Into the Properties of Monomeric Insulin. Acta Crystallogr.,Sect.D, 62:505-, 2006 Cited by PubMed Abstract: Despentapeptide (des-B26-B30) insulin (DPI), an active modified insulin, has been crystallized in the presence of 20% acetic acid pH 2. A crystal structure analysis to 1.8 A spacing (space group I222) revealed that the DPI molecule, which is unable to make beta-strand interactions for physiological dimer formation and is apparently monomeric in solution, formed an alternative lattice-generated dimer. The formation of this dimer involved interactions between surfaces which included the B9-B19 alpha-helices (usually buried by the dimer-dimer contacts within the native hexamer). The two crystallographically independent molecules within the dimer were essentially identical and were similar in conformation to T-state insulin as seen in the T(6) insulin hexamer. An unusual feature of each molecule in the dimer was the presence of two independent conformations at the B-chain C-terminus (residues B20-B25). Both conformations were different from that of native insulin, involving a 3.5 A displacement of the B20-B23 beta-turn and a repositioning of residue PheB25 such that it made close van der Waals contact with the main body of the molecule, appearing to stabilize the B-chain C-terminus. PubMed: 16627943DOI: 10.1107/S0907444906006871 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
