2RRI
NMR structure of vasoactive intestinal peptide in DPC Micelle
Summary for 2RRI
| Entry DOI | 10.2210/pdb2rri/pdb |
| NMR Information | BMRB: 11420 |
| Descriptor | Vasoactive intestinal peptide (1 entity in total) |
| Functional Keywords | hormone |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P01282 |
| Total number of polymer chains | 1 |
| Total formula weight | 3389.88 |
| Authors | Umetsu, Y.,Tenno, T.,Goda, N.,Shirakawa, M.,Ikegami, T.,Hiroaki, H. (deposition date: 2010-12-21, release date: 2011-04-06, Last modification date: 2024-05-15) |
| Primary citation | Umetsu, Y.,Tenno, T.,Goda, N.,Shirakawa, M.,Ikegami, T.,Hiroaki, H. Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments Biochim.Biophys.Acta, 1814:724-730, 2011 Cited by PubMed Abstract: Vasoactive intestinal peptide (VIP) is a 28-amino acid neuropeptide which belongs to a glucagon/secretin superfamily, the ligand of class II G protein-coupled receptors. Knowledge for the conformation of VIP bound to membrane is important because the receptor activation is initiated by membrane binding of VIP. We have previously observed that VIP-G (glycine-extended VIP) is unstructured in solution, as evidenced by the limited NMR chemical shift dispersion. In this study, we determined the three-dimensional structures of VIP-G in two distinct membrane-mimicking environments. Although these are basically similar structures composed of a disordered N-terminal region and a long α-helix, micelle-bound VIP-G has a curved α-helix. The side chains of residues Phe(6), Tyr(10), Leu(13), and Met(17) found at the concave face form a hydrophobic patch in the micelle-bound state. The structural differences in two distinct membrane-mimicking environments show that the micelle-bound VIP-G localized at the water-micelle boundary with these side chains toward micelle interior. In micelle-bound PACAP-38 (one of the glucagon/secretin superfamily peptide) structure, the identical hydrophobic residues form the micelle-binding interface. This result suggests that these residues play an important role for the membrane binding of VIP and PACAP. PubMed: 21439408DOI: 10.1016/j.bbapap.2011.03.009 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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