1gt1: Difference between revisions

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 (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.

1GT1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with PRZ and ANC as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: PRZ. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GT1 OCA].  

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