View source for 2lfo


==NMR structure of cl-BABP/SS complexed with glycochenodeoxycholic and glycocholic acids==
<StructureSection load='2lfo' size='340' side='right'caption='[[2lfo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lfo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LFO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHO:GLYCOCHENODEOXYCHOLIC+ACID'>CHO</scene>, <scene name='pdbligand=GCH:GLYCOCHOLIC+ACID'>GCH</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=2lfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lfo OCA], [https://pdbe.org/2lfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lfo RCSB], [https://www.ebi.ac.uk/pdbsum/2lfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lfo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABPL_CHICK FABPL_CHICK] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The presence of a disulfide bridge in liver bile acid binding protein (L-BABP/S-S) allows for site-selective binding of two bile acids, glycochenodeoxycholic (GCDA) and glycocholic acid (GCA), differing only in the presence of a hydroxyl group. The protein form devoid of the disulfide bridge (L-BABP) binds both bile salts without discriminating ability. We investigate the determinants of the molecular recognition process in the formation of the heterotypic L-BABP/S-S complex with GCA and GCDA located in the superficial and inner protein sites, respectively. The comparison of the NMR spectroscopy structure of heterotypic holo L-BABP/S-S, the first reported for this protein family, with that of the homotypic L-BABP complex demonstrates that the introduction of a S-S link between adjacent strands changes the conformation of three key residues, which function as hot-spot mediators of molecular discrimination. The favoured chi(1) rotameric states (t, g(+) and g(-) for E99, Q100 and E109 residues, respectively) allow the onset of an extended intramolecular hydrogen-bond network and the consequent stabilisation of the side-chain orientation of a buried histidine, which is capable of anchoring a specific ligand.

A disulfide bridge allows for site-selective binding in liver bile acid binding protein thereby stabilising the orientation of key amino acid side chains.,Tomaselli S, Assfalg M, Pagano K, Cogliati C, Zanzoni S, Molinari H, Ragona L Chemistry. 2012 Mar 5;18(10):2857-66. doi: 10.1002/chem.201102203. Epub 2012 Feb , 1. PMID:22298334<ref>PMID:22298334</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lfo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Assfalg M]]
[[Category: Cogliati C]]
[[Category: Molinari H]]
[[Category: Pagano K]]
[[Category: Ragona L]]
[[Category: Tomaselli S]]
[[Category: Zanzoni S]]
[[Category: Zetta L]]