View source for 4run


==Crystal structure of human odorant binding protein OBPIIa==
<StructureSection load='4run' size='340' side='right'caption='[[4run]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4run]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RUN 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=4run FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4run OCA], [https://pdbe.org/4run PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4run RCSB], [https://www.ebi.ac.uk/pdbsum/4run PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4run ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OBP2A_HUMAN OBP2A_HUMAN] Probably binds and transports small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids.<ref>PMID:12044155</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human odorant-binding protein, OBPIIa , is expressed by nasal epithelia to facilitate transport of hydrophobic odorant molecules across the aqueous mucus. Here, we report its crystallographic analysis at 2.6 A resolution. OBPIIa is a monomeric protein that exhibits the classical lipocalin fold with a conserved eight-stranded beta-barrel harboring a remarkably large hydrophobic pocket. Basic residues within the four loops that shape the entrance to this ligand-binding site evoke a positive electrostatic potential. Human OBPIIa shows distinct features compared with other mammalian OBPs, including a potentially reactive Cys side chain within its pocket similar to human tear lipocalin. Proteins 2015. (c) 2015 Wiley Periodicals, Inc.

Crystal structure of the human odorant binding protein, OBP.,Schiefner A, Freier R, Eichinger A, Skerra A Proteins. 2015 Mar 21. doi: 10.1002/prot.24797. PMID:25810031<ref>PMID:25810031</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4run" style="background-color:#fffaf0;"></div>

==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Schiefner A]]
[[Category: Skerra A]]