1exs
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1exs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXS FirstGlance]. <br> | <table><tr><td colspan='2'>[[1exs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXS FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.39Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1exs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exs OCA], [https://pdbe.org/1exs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exs RCSB], [https://www.ebi.ac.uk/pdbsum/1exs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exs 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=1exs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exs OCA], [https://pdbe.org/1exs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exs RCSB], [https://www.ebi.ac.uk/pdbsum/1exs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/LACB_PIG LACB_PIG] Lactoglobulin is the 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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1exs ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1exs ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | beta-Lactoglobulin (BLG) is a lipocalin and is the major protein in the whey of the milk of cows and other ruminants, but not in all mammalian species. The biological function of BLG is not clear, but a potential role in carrying fatty acids through the digestive tract has been proposed. The capability of BLG to aggregate and form gels is often used to thicken foodstuffs. The structure of the porcine form is sufficiently different from other known BLG structures that SIRAS phases had to be measured in order to solve the crystal structure to 2.4 A resolution. The r.m.s. deviation of C(alpha) atoms is 2.8 A between porcine and bovine BLG. Nevertheless, the typical lipocalin fold is conserved. Compared with bovine BLG, the tilted alpha-helix alters the arrangement of surface residues of the porcine form, completely changing the dimerization behaviour. Through a unique pH-dependent domain-swapping mechanism involving the first ten residues, a novel dimer interface is formed at the N-terminus of porcine BLG. The existence of this novel dimer at low pH is supported by gel-filtration experiments. These results provide a rationale for the difference in physicochemical behaviour between bovine and porcine BLG and point the way towards engineering such dimerization motifs into other members of the lipocalin family. | ||
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| - | A novel pH-dependent dimerization motif in beta-lactoglobulin from pig (Sus scrofa).,Hoedemaeker FJ, Visschers RW, Alting AC, de Kruif KG, Kuil ME, Abrahams JP Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):480-6. Epub 2002, Feb 21. PMID:11856834<ref>PMID:11856834</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1exs" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | *[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Abrahams | + | [[Category: Abrahams JP]] |
| - | [[Category: Hoedemaeker | + | [[Category: Hoedemaeker FJ]] |
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Revision as of 10:07, 20 March 2024
STRUCTURE OF PORCINE BETA-LACTOGLOBULIN
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