View source for 1ooh


==Complex of Drosophila odorant binding protein LUSH with butanol==
<StructureSection load='1ooh' size='340' side='right'caption='[[1ooh]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ooh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OOH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1BO:1-BUTANOL'>1BO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ooh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ooh OCA], [https://pdbe.org/1ooh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ooh RCSB], [https://www.ebi.ac.uk/pdbsum/1ooh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ooh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OB76A_DROME OB76A_DROME] Odorant-binding protein required for olfactory behavior and for activity of pheromone-sensitive neurons. Binds to alcohols and mediates avoidance behavior to high concentrations of alcohols, the alcohol-binding possibly resulting in activation of receptors on T2B neurons, the activation of these receptors inhibiting these neurons. Acts in concert with Snmp and lush to capture cVA molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. Required for cVA response, probably by binding to VA. May act by serving as an adapter that bridges the presence of gaseous pheromone molecules, cVA, to activation of specific neuronal receptors expressed on T1 olfactory neurons, possibly via a specific conformational change induced by cVA that in turn activates T1 receptors. T1 neurons are excited by the pheromone VA, while T2 neurons are inhibited by alcohols. Also binds to phthalates.<ref>PMID:9755202</ref> <ref>PMID:11238251</ref> <ref>PMID:14759510</ref> <ref>PMID:15664171</ref> <ref>PMID:16928861</ref> <ref>PMID:17943085</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oo/1ooh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ooh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have solved the high-resolution crystal structures of the Drosophila melanogaster alcohol-binding protein LUSH in complex with a series of short-chain n-alcohols. LUSH is the first known nonenzyme protein with a defined in vivo alcohol-binding function. The structure of LUSH reveals a set of molecular interactions that define a specific alcohol-binding site. A group of amino acids, Thr57, Ser52 and Thr48, form a network of concerted hydrogen bonds between the protein and the alcohol that provides a structural motif to increase alcohol-binding affinity at this site. This motif seems to be conserved in a number of mammalian ligand-gated ion channels that are directly implicated in the pharmacological effects of alcohol. Further, these sequences are found in regions of ion channels that are known to confer alcohol sensitivity. We suggest that the alcohol-binding site in LUSH represents a general model for alcohol-binding sites in proteins.

Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster.,Kruse SW, Zhao R, Smith DP, Jones DN Nat Struct Biol. 2003 Sep;10(9):694-700. Epub 2003 Jul 27. PMID:12881720<ref>PMID:12881720</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ooh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Jones DNM]]
[[Category: Kruse SW]]
[[Category: Smith DP]]
[[Category: Zhao R]]