1c98
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SOLUTION STRUCTURE OF NEUROMEDIN B
OverviewOverview
The solution structure of neuromedin B (NMB) was investigated using, two-dimensional nuclear magnetic resonance (NMR) spectroscopy in, membrane-mimicking environments. NMB adopts a relaxed helical conformation, from Trp(4) to Met(10) in 50% aqueous 2,2, 2-trifluoroethanol (TFE), solution and in 150 mM SDS micelles. Sidechain atoms of the three, residues, Trp(4), His(8) and Phe(9) orient toward the same direction and, these residues might play a key role on interacting with hydrophobic acyl, chains of the phospholipids in the membrane. NOESY experiments performed, on NMB in non-deuterated SDS micelle show that aromatic ring protons of, Trp(4) and Phe(9) residues are in close contact with methylene protons of, SDS micelles. In addition, proton longitudinal relaxation data proved that, the interactions between NMB with SDS micelle are characterized as, extrinsic interaction. Trp(4) and Phe(9) seem to be important in, interaction with receptor and this agrees with the previous studies of, structure-activity relationship (Howell, D.C. et al. (1996) Int. J. Pept., Protein Res. 48, 522-531). These conformational features might be helpful, in understanding the molecular mechanism of the function of NMB and, developing the efficient drugs.
About this StructureAbout this Structure
1C98 is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of neuromedin B by (1)H nuclear magnetic resonance spectroscopy., Lee S, Kim Y, FEBS Lett. 1999 Oct 29;460(2):263-9. PMID:10544247
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