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| | <StructureSection load='3nq3' size='340' side='right'caption='[[3nq3]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3nq3' size='340' side='right'caption='[[3nq3]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nq3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NQ3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NQ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nq3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NQ3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3npo|3npo]], [[3nq9|3nq9]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3nq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nq3 OCA], [http://pdbe.org/3nq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nq3 RCSB], [http://www.ebi.ac.uk/pdbsum/3nq3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nq3 ProSAT]</span></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=3nq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nq3 OCA], [https://pdbe.org/3nq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nq3 RCSB], [https://www.ebi.ac.uk/pdbsum/3nq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nq3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN]] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. | + | [https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lewinski, K]] | + | [[Category: Lewinski K]] |
| - | [[Category: Loch, J]] | + | [[Category: Loch J]] |
| - | [[Category: Beta-lactoglobulin]]
| + | |
| - | [[Category: Bovine milk]]
| + | |
| - | [[Category: Capric acid]]
| + | |
| - | [[Category: Decanoic acid]]
| + | |
| - | [[Category: Fatty acid]]
| + | |
| - | [[Category: Lipocalin]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
LACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lactoglobulin is a natural protein present in bovine milk and common component of human diet, known for binding with high affinity wide range of hydrophobic compounds, among them fatty acids 12-20 carbon atoms long. Shorter fatty acids were reported as not binding to beta-lactoglobulin. We used X-ray crystallography and fluorescence spectroscopy to show that lactoglobulin binds also 8- and 10-carbon caprylic and capric acids, however with lower affinity. The determined apparent association constant for lactoglobulin complex with caprylic acid is 10.8 +/- 1.7 x 10(3) M(-1) , while for capric acid is 6.0 +/- 0.5 x 10(3) M(-1) . In crystal structures determined with resolution 1.9 A the caprylic acid is bound in upper part of central calyx near polar residues located at CD loop, while the capric acid is buried deeper in the calyx bottom and does not interact with polar residues at CD loop. In both structures, water molecule hydrogen-bonded to carboxyl group of fatty acid is observed. Different location of ligands in the binding site indicates that competition between polar and hydrophobic interactions is an important factor determining position of the ligand in beta-barrel. Copyright (c) 2010 John Wiley & Sons, Ltd.
Two modes of fatty acid binding to bovine beta-lactoglobulin-crystallographic and spectroscopic studies.,Loch J, Polit A, Gorecki A, Bonarek P, Kurpiewska K, Dziedzicka-Wasylewska M, Lewinski K J Mol Recognit. 2011 Mar;24(2):341-9. doi: 10.1002/jmr.1084. Epub 2010 Dec, 14. PMID:21360616[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Loch J, Polit A, Gorecki A, Bonarek P, Kurpiewska K, Dziedzicka-Wasylewska M, Lewinski K. Two modes of fatty acid binding to bovine beta-lactoglobulin-crystallographic and spectroscopic studies. J Mol Recognit. 2011 Mar;24(2):341-9. doi: 10.1002/jmr.1084. Epub 2010 Dec, 14. PMID:21360616 doi:10.1002/jmr.1084
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