2hnx

<StructureSection load='2hnx' size='340' side='right' caption='[[2hnx]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[2hnx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HNX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2hnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hnx OCA], [http://pdbe.org/2hnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hnx RCSB], [http://www.ebi.ac.uk/pdbsum/2hnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hnx ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FABP4_HUMAN FABP4_HUMAN]] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity).

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== Publication Abstract from PubMed ==

Human adipocyte lipid-binding protein (aP2) belongs to a family of intracellular lipid-binding proteins involved in the transport and storage of lipids. Here, the crystal structure of human aP2 with a bound palmitate is described at 1.5 A resolution. Unlike the known crystal structure of murine aP2 in complex with palmitate, this structure shows that the fatty acid is in a folded conformation and that the loop containing Phe57 acts as a lid to regulate ligand binding by excluding solvent exposure to the central binding cavity.

Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).,Marr E, Tardie M, Carty M, Brown Phillips T, Wang IK, Soeller W, Qiu X, Karam G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1058-60. Epub 2006 Oct 25. PMID:17077479<ref>PMID:17077479</ref>

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

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<div class="pdbe-citations 2hnx" style="background-color:#fffaf0;"></div>

*[[Fatty acid-binding protein|Fatty acid-binding protein]]

[[Category: Human]]

[[Category: Carty, M]]

[[Category: Karam, G]]

[[Category: Marr, E]]

[[Category: Phillips, T Brown]]

[[Category: Qiu, X]]

[[Category: Tardie, M]]

[[Category: Fatty acid binding protein]]

[[Category: Lipid binding protein]]