4ck4

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'''Unreleased structure'''
 
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The entry 4ck4 is ON HOLD
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==Ovine beta-Lactoglobulin at Atomic Resolution==
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<StructureSection load='4ck4' size='340' side='right'caption='[[4ck4]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ck4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CK4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.12&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ck4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ck4 OCA], [https://pdbe.org/4ck4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ck4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ck4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ck4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LACB_SHEEP LACB_SHEEP] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the triclinic form of the milk protein beta-lactoglobulin from sheep (Ovis aries) at 1.1 A resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.
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Authors: Kontopidis, G., Nordle, A., Sawyer, L.
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Ovine beta-lactoglobulin at atomic resolution.,Kontopidis G, Nordle Gilliver A, Sawyer L Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1498-503. doi:, 10.1107/S2053230X14020950. Epub 2014 Oct 31. PMID:25372816<ref>PMID:25372816</ref>
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Description: Ovine beta-Lactoglobulin at Atomic Resolution
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ck4" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Ovis aries]]
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[[Category: Kontopidis G]]
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[[Category: Nordle A]]
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[[Category: Sawyer L]]

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Ovine beta-Lactoglobulin at Atomic Resolution

PDB ID 4ck4

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