4zh9: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 4zh9 is ON HOLD
+==Crystal Structure of the Domain-Swapped Dimer Wild-Type of Human Cellular Retinol Binding Protein II==
+<StructureSection load='4zh9' size='340' side='right'caption='[[4zh9]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4zh9]] 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=4ZH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZH9 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.66&#8491;</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=4zh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zh9 OCA], [https://pdbe.org/4zh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zh9 RCSB], [https://www.ebi.ac.uk/pdbsum/4zh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zh9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN] Intracellular transport of retinol.
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Assar, Z., Nossoni, Z., Geiger, J.H.
+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>
-Description: Crystal Structure of the Domain-Swapped Dimer Wild-Type of Human Cellular Retinol Binding Protein II
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Geiger, J.H]]
+<div class="pdbe-citations 4zh9" style="background-color:#fffaf0;"></div>
-[[Category: Nossoni, Z]]
-[[Category: Assar, Z]]
+==See Also==
+*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Assar Z]]
+[[Category: Geiger JH]]
+[[Category: Nossoni Z]]