4run: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Crystal structure of human odorant binding protein OBPIIa==

== Structural highlights ==

<table><tr><td colspan='2'>[[4run]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RUN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4run FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4run OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4run RCSB], [http://www.ebi.ac.uk/pdbsum/4run PDBsum]</span></td></tr>

</table>

== Function ==

[[http://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>

== 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.

~~The entry 4run is ON HOLD until Paper Publication~~

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>

~~Authors: Schiefner~~, A.~~, Skerra, A~~.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

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

== References ==

[[Category: ~~Unreleased Structures~~]]

__TOC__

</StructureSection>

[[Category: Schiefner, A]]

[[Category: Skerra, A]]

[[Category: ~~Schiefner, A~~]]

[[Category: Aliphatic aldehyde]]

[[Category: Fatty acid]]

[[Category: Human lipocalin]]

[[Category: Lilial]]

[[Category: Lipid binding protein]]

[[Category: Nasal mucus]]

[[Category: Odorant-binding protein]]

[[Category: Transport protein]]

[[Category: Vanillin]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RUN FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4run FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4run OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4run RCSB], [http://www.ebi.ac.uk/pdbsum/4run PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://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.
-The entry 4run is ON HOLD  until Paper Publication
+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>
-Authors: Schiefner, A., Skerra, A.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of human odorant binding protein OBPIIa
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Schiefner, A]]
 [[Category: Skerra, A]]
-[[Category: Schiefner, A]]
+[[Category: Aliphatic aldehyde]]
+[[Category: Fatty acid]]
+[[Category: Human lipocalin]]
+[[Category: Lilial]]
+[[Category: Lipid binding protein]]
+[[Category: Nasal mucus]]
+[[Category: Odorant-binding protein]]
+[[Category: Transport protein]]
+[[Category: Vanillin]]