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| | ==NMR structure of cl-BABP/SS complexed with glycochenodeoxycholic and glycocholic acids== | | ==NMR structure of cl-BABP/SS complexed with glycochenodeoxycholic and glycocholic acids== |
| - | <StructureSection load='2lfo' size='340' side='right' caption='[[2lfo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lfo' size='340' side='right'caption='[[2lfo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LFO FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHO:GLYCOCHENODEOXYCHOLIC+ACID'>CHO</scene>, <scene name='pdbligand=GCH:GLYCOCHOLIC+ACID'>GCH</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jn3|2jn3]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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> |
| - | <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=2lfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lfo OCA], [http://pdbe.org/2lfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lfo RCSB], [http://www.ebi.ac.uk/pdbsum/2lfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lfo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Fatty acid-binding protein|Fatty acid-binding protein]] | + | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Assfalg, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Cogliati, C]] | + | [[Category: Assfalg M]] |
| - | [[Category: Molinari, H]] | + | [[Category: Cogliati C]] |
| - | [[Category: Pagano, K]] | + | [[Category: Molinari H]] |
| - | [[Category: Ragona, L]] | + | [[Category: Pagano K]] |
| - | [[Category: Tomaselli, S]] | + | [[Category: Ragona L]] |
| - | [[Category: Zanzoni, S]] | + | [[Category: Tomaselli S]] |
| - | [[Category: Zetta, L]] | + | [[Category: Zanzoni S]] |
| - | [[Category: Bile acid binding protein]]
| + | [[Category: Zetta L]] |
| - | [[Category: Bile acid]]
| + | |
| - | [[Category: Disulphide bridge]]
| + | |
| - | [[Category: Heterotypic complex]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Liver]]
| + | |
| Structural highlights
Function
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tomaselli S, Assfalg M, Pagano K, Cogliati C, Zanzoni S, Molinari H, Ragona L. A disulfide bridge allows for site-selective binding in liver bile acid binding protein thereby stabilising the orientation of key amino acid side chains. Chemistry. 2012 Mar 5;18(10):2857-66. doi: 10.1002/chem.201102203. Epub 2012 Feb , 1. PMID:22298334 doi:10.1002/chem.201102203
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