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| | <StructureSection load='4zh6' size='340' side='right'caption='[[4zh6]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='4zh6' size='340' side='right'caption='[[4zh6]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zh6]] is a 1 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=4ZH6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZH6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zh6]] is a 1 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=4ZH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZH6 FirstGlance]. <br> |
| - | </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> | + | </td></tr><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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qzt|4qzt]], [[4qzu|4qzu]], [[4qyp|4qyp]], [[4qyn|4qyn]]</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=4zh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zh6 OCA], [https://pdbe.org/4zh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zh6 RCSB], [https://www.ebi.ac.uk/pdbsum/4zh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zh6 ProSAT]</span></td></tr> |
| - | <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>
| + | |
| - | <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=4zh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zh6 OCA], [http://pdbe.org/4zh6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zh6 RCSB], [http://www.ebi.ac.uk/pdbsum/4zh6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zh6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN]] Intracellular transport of retinol. | + | [https://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN] Intracellular transport of retinol. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Assar, Z]] | + | [[Category: Assar Z]] |
| - | [[Category: Geiger, J H]] | + | [[Category: Geiger JH]] |
| - | [[Category: Nossoni, Z]] | + | [[Category: Nossoni Z]] |
| - | [[Category: Domain swapping]]
| + | |
| - | [[Category: Domain-swapped dimer]]
| + | |
| - | [[Category: Human cellular retinol binding protein ii]]
| + | |
| - | [[Category: Intracellular lipid binding protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
RET2_HUMAN Intracellular transport of retinol.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Assar Z, Nossoni Z, Wang W, Santos EM, Kramer K, McCornack C, Vasileiou C, Borhan B, Geiger JH. Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates. Structure. 2016 Sep 6;24(9):1590-8. doi: 10.1016/j.str.2016.05.022. Epub 2016 Aug, 11. PMID:27524203 doi:http://dx.doi.org/10.1016/j.str.2016.05.022
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