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5dg4

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<StructureSection load='5dg4' size='340' side='right'caption='[[5dg4]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='5dg4' size='340' side='right'caption='[[5dg4]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dg4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DG4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dg4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DG4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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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]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RBP2, CRBP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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></td></tr>
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<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=5dg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dg4 OCA], [http://pdbe.org/5dg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dg4 RCSB], [http://www.ebi.ac.uk/pdbsum/5dg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dg4 ProSAT]</span></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=5dg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dg4 OCA], [https://pdbe.org/5dg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dg4 RCSB], [https://www.ebi.ac.uk/pdbsum/5dg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dg4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN]] Intracellular transport of retinol.
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[https://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN] Intracellular transport of retinol.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human Cellular Retinol Binding Protein II (hCRBPII), a member of the intracellular lipid-binding protein family, is a monomeric protein responsible for the intracellular transport of retinol and retinal. Herein we report that hCRBPII forms an extensive domain-swapped dimer during bacterial expression. The domain-swapped region encompasses almost half of the protein. The dimer represents a novel structural architecture with the mouths of the two binding cavities facing each other, producing a new binding cavity that spans the length of the protein complex. Although wild-type hCRBPII forms the dimer, the propensity for dimerization can be substantially increased via mutation at Tyr60. The monomeric form of the wild-type protein represents the thermodynamically more stable species, making the domain-swapped dimer a kinetically trapped entity. Hypothetically, the wild-type protein has evolved to minimize dimerization of the folding intermediate through a critical hydrogen bond (Tyr60-Glu72) that disfavors the dimeric form.
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Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.,Assar Z, Nossoni Z, Wang W, Santos EM, Kramer K, McCornack C, Vasileiou C, Borhan B, Geiger JH Structure. 2016 Sep 6;24(9):1590-8. doi: 10.1016/j.str.2016.05.022. Epub 2016 Aug, 11. PMID:27524203<ref>PMID:27524203</ref>
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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 5dg4" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Assar, Z]]
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[[Category: Assar Z]]
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[[Category: Borhan, B]]
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[[Category: Borhan B]]
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[[Category: Gieger, J H]]
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[[Category: Gieger JH]]
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[[Category: Nossoni, Z]]
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[[Category: Nossoni Z]]
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[[Category: Wang, W]]
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[[Category: Wang W]]
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[[Category: Domain swapping]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of monomer human cellular retinol binding protein II-Y60L

PDB ID 5dg4

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