1LBJ
NMR solution structure of motilin in phospholipid bicellar solution
Summary for 1LBJ
| Entry DOI | 10.2210/pdb1lbj/pdb |
| NMR Information | BMRB: 5454 |
| Descriptor | motilin (1 entity in total) |
| Functional Keywords | a-helix, b-turn of type i, hormone-growth factor complex, hormone/growth factor |
| Cellular location | Secreted: P12872 |
| Total number of polymer chains | 1 |
| Total formula weight | 2703.08 |
| Authors | Andersson, A.,Maler, L. (deposition date: 2002-04-03, release date: 2002-11-20, Last modification date: 2024-05-22) |
| Primary citation | Andersson, A.,Maler, L. NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution J.BIOMOL.NMR, 24:103-112, 2002 Cited by PubMed Abstract: The structure and dynamics of the gastrointestinal peptide hormone motilin, consisting of 22 amino acid residues, have been studied in the presence of isotropic q = 0.5 phospholipid bicelles. The NMR solution structure of the peptide in acidic bicelle solution was determined from 203 NOE-derived distance constraints and six backbone torsion angle constraints. Dynamic properties for the 13Calpha-1H vector in Leu10 were determined for motilin specifically labeled with 13C at this position by analysis of multiple-field relaxation data. The structure reveals an ordered alpha-helical conformation between Glu9 and Lys20. The N-terminus is also well structured with a turn resembling that of a classical beta-turn. The 13C dynamics clearly show that motilin tumbles slowly in solution, with a correlation time characteristic of a large object. It was also found that motilin has a large degree of local flexibility as compared with what has previously been reported in SDS micelles. The results show that motilin interacts with the bicelle, displaying motional properties of a peptide bound to a membrane. In comparison, motilin in neutral bicelles seems less structured and more flexible. This study shows that the small isotropic bicelles are well suited for use as membrane-mimetic for structural as well as dynamical investigations of membrane-bound peptides by high-resolution NMR. PubMed: 12495026DOI: 10.1023/A:1020902915969 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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