1gt4: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gt4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GT4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gt4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GT4 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNA:UNDECANAL'>UNA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNA:UNDECANAL'>UNA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g85|1g85]], [[1gt1|1gt1]], [[1gt3|1gt3]], [[1gt5|1gt5]], [[1hn2|1hn2]], [[1obp|1obp]], [[1pbo|1pbo]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g85|1g85]], [[1gt1|1gt1]], [[1gt3|1gt3]], [[1gt5|1gt5]], [[1hn2|1hn2]], [[1obp|1obp]], [[1pbo|1pbo]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gt4 RCSB], [http://www.ebi.ac.uk/pdbsum/1gt4 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gt4 RCSB], [http://www.ebi.ac.uk/pdbsum/1gt4 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Cambillau, C | [[Category: Cambillau, C]] | ||
[[Category: Conti, V | [[Category: Conti, V]] | ||
[[Category: Grolli, S | [[Category: Grolli, S]] | ||
[[Category: Ramoni, R | [[Category: Ramoni, R]] | ||
[[Category: Spinelli, S | [[Category: Spinelli, S]] | ||
[[Category: Tegoni, M | [[Category: Tegoni, M]] | ||
[[Category: Vincent, F | [[Category: Vincent, F]] | ||
[[Category: Lipocalin]] | [[Category: Lipocalin]] | ||
[[Category: Odorant-binding protein]] | [[Category: Odorant-binding protein]] | ||
Revision as of 00:31, 23 December 2014
Complex of Bovine Odorant Binding Protein with undecanalComplex of Bovine Odorant Binding Protein with undecanal
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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