1gt3: Difference between revisions

Revision as of 06:01, 1 July 2008

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File:1gt3.png

Template:STRUCTURE 1gt3

COMPLEX OF BOVINE ODORANT BINDING PROTEIN WITH DIHYDROMYRCENOLCOMPLEX OF BOVINE ODORANT BINDING PROTEIN WITH DIHYDROMYRCENOL

Template:ABSTRACT PUBMED 15373829

About this StructureAbout this Structure

1GT3 is a Single protein structure of sequence from Bos taurus. 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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-'''COMPLEX OF BOVINE ODORANT BINDING PROTEIN WITH DIHYDROMYRCENOL'''
+===COMPLEX OF BOVINE ODORANT BINDING PROTEIN WITH DIHYDROMYRCENOL===
-==Overview==
+<!--
-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. &amp; Cambillau, C. (1996) Nat. Struct. Biol.3, 863-867; Bianchet, M.A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S.H., Monaco, H.L. &amp; 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. &amp; 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 (pOBP), although the latter is monomeric and devoid of ligand when purified. The odorant molecules presented K(d) values with bOBP in the micromolar range. Most of the X-ray structures revealed that odorant molecules interact with a common set of residues forming the cavity wall and do not exhibit specific interactions. Depending on the ligand and on the monomer (A or B), a single residue--Phe89--presents alternate conformations and might control cross-talking between the subunits. Crystal data on both pOBP and bOBP, in contrast with binding and spectroscopic studies on rat OBP in solution, reveal an absence of significant conformational changes involving protein loops or backbone. Thus, the role of OBP in signal triggering remains unresolved.
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 [[Category: Bovine odorant binding protein]]
 [[Category: Lipocalin]]
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