COMPLEX OF BOVINE ODORANT BINDING PROTEIN WITH DIHYDROMYRCENOL

File:1gt3.gif


1gt3, resolution 1.8Å

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OverviewOverview

The structure of bovine odorant-binding protein (bOBP) revealed a striking, feature of a dimer formed by domain swapping [Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. & Cambillau, C. (1996) Nat. Struct. Biol.3, 863-867; Bianchet, M.A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S.H., Monaco, H.L. & Amzel, L.M. (1996) Nat. Struct. Biol.3, 934-939] and the, presence of a naturally occuring ligand [Ramoni, R., Vincent, F., Grolli, S., Conti, V., Malosse, C., Boyer, F.D., Nagnan-Le Meillour, P., Spinelli, S., Cambillau, C. & Tegoni, M. (2001) J. Biol. Chem.276, 7150-7155]. These, features led us to investigate the binding of odorant molecules with bOBP, in solution and in the crystal. The behavior of odorant molecules in bOBP, resembles that observed with porcine OBP ... [(full description)]

About this StructureAbout this Structure

1GT3 is a [Single protein] structure of sequence from [Bos taurus] with DHM and 3OL as [ligands]. Structure known Active Site: DHA. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structures of bovine odorant-binding protein in complex with odorant molecules., Vincent F, Ramoni R, Spinelli S, Grolli S, Tegoni M, Cambillau C, Eur J Biochem. 2004 Oct;271(19):3832-42. PMID:15373829

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