1gt3: Difference between revisions
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<StructureSection load='1gt3' size='340' side='right'caption='[[1gt3]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1gt3' size='340' side='right'caption='[[1gt3]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gt3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1gt3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GT3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3OM:(3S)-1-OCTEN-3-OL'>3OM</scene>, <scene name='pdbligand=DHM:2,6-DIMETHYL-7-OCTEN-2-OL'>DHM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3OM:(3S)-1-OCTEN-3-OL'>3OM</scene>, <scene name='pdbligand=DHM:2,6-DIMETHYL-7-OCTEN-2-OL'>DHM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g85|1g85]], [[1gt1|1gt1]], [[1gt4|1gt4]], [[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"><div style='overflow: auto; max-height: 3em;'>[[1g85|1g85]], [[1gt1|1gt1]], [[1gt4|1gt4]], [[1gt5|1gt5]], [[1hn2|1hn2]], [[1obp|1obp]], [[1pbo|1pbo]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt3 OCA], [https://pdbe.org/1gt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gt3 RCSB], [https://www.ebi.ac.uk/pdbsum/1gt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gt3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/OBP_BOVIN OBP_BOVIN]] This protein binds a wide variety of chemical odorants. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]] | *[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]] | ||
== References == | == References == | ||
Revision as of 14:28, 28 July 2021
Complex of Bovine Odorant Binding Protein with dihydromyrcenolComplex of Bovine Odorant Binding Protein with dihydromyrcenol
Structural highlights
Function[OBP_BOVIN] This protein binds a wide variety of chemical odorants. 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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