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| ==Bovine beta-lactoglobulin complex with palmitic acid== | | ==Bovine beta-lactoglobulin complex with palmitic acid== |
- | <StructureSection load='3uew' size='340' side='right' caption='[[3uew]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3uew' size='340' side='right'caption='[[3uew]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3uew]] 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=3UEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UEW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3uew]] 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=3UEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UEW FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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]] 2Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ueu|3ueu]], [[3uev|3uev]], [[3uex|3uex]], [[3npo|3npo]], [[3nq3|3nq3]], [[3nq9|3nq9]], [[3qzk|3qzk]], [[3qzj|3qzj]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=3uew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uew OCA], [http://pdbe.org/3uew PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uew RCSB], [http://www.ebi.ac.uk/pdbsum/3uew PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uew 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=3uew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uew OCA], [https://pdbe.org/3uew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uew RCSB], [https://www.ebi.ac.uk/pdbsum/3uew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uew 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. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| </div> | | </div> |
| <div class="pdbe-citations 3uew" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3uew" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
- | [[Category: Lewinski, K]] | + | [[Category: Large Structures]] |
- | [[Category: Loch, J]] | + | [[Category: Lewinski K]] |
- | [[Category: Beta barrel]] | + | [[Category: Loch J]] |
- | [[Category: Beta protein]]
| + | |
- | [[Category: Bovine milk]]
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- | [[Category: Lipocalin]]
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- | [[Category: Transport protein]]
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| Structural highlights
Function
LACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
Publication Abstract from PubMed
Lactoglobulin is a globular milk protein for which physiological function has not been clarified. Due to its binding properties lactoglobulin might serve as a carrier for bioactive molecules. Binding of 12-, 14-, 16- and 18-carbon saturated fatty acids to bovine beta-lactoglobulin has been characterised by isothermal titration calorimetry and X-ray crystallography as a part of systematic studies of lactoglobulin complexes with ligands of biological importance. The thermodynamic parameters have been determined for lauric, myristic and palmitic acid complexes revealing systematic decrease of enthalpic and increase of entropic component of DeltaG with elongation of aliphatic chain. In all crystal structures determined with resolution 1.9-2.1A, single fatty acid molecule was found in the beta-barrel in extended conformation with individual pattern of interactions. Location of a fatty acid in the binding site depends on the length of aliphatic chain and influences polar interactions between protein and ligand. Systematic changes of entropic component indicate important role of water in binding process.
Structural and thermodynamic studies of binding saturated fatty acids to bovine beta-lactoglobulin.,Loch JI, Polit A, Bonarek P, Olszewska D, Kurpiewska K, Dziedzicka-Wasylewska M, Lewinski K Int J Biol Macromol. 2012 Mar 10. PMID:22425630[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Loch JI, Polit A, Bonarek P, Olszewska D, Kurpiewska K, Dziedzicka-Wasylewska M, Lewinski K. Structural and thermodynamic studies of binding saturated fatty acids to bovine beta-lactoglobulin. Int J Biol Macromol. 2012 Mar 10. PMID:22425630 doi:10.1016/j.ijbiomac.2012.03.002
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