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New page: '''Unreleased structure''' The entry 4run is ON HOLD Authors: Schiefner, A., Skerra, A. Description: Crystal structure of human odorant binding protein OBPIIa
 
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'''Unreleased structure'''


The entry 4run is ON HOLD
==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.


Authors: Schiefner, A., Skerra, A.
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>


Description: Crystal structure of human odorant binding protein OBPIIa
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]]
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