4zgu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:15, 6 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of monomer Y60W hCRBPII==
==Crystal structure of monomer Y60W hCRBPII==
-
<StructureSection load='4zgu' size='340' side='right' caption='[[4zgu]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
+
<StructureSection load='4zgu' size='340' side='right'caption='[[4zgu]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4zgu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZGU FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4zgu]] 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=4ZGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZGU 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</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=4zgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgu OCA], [http://pdbe.org/4zgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zgu RCSB], [http://www.ebi.ac.uk/pdbsum/4zgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zgu ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zgu OCA], [https://pdbe.org/4zgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zgu RCSB], [https://www.ebi.ac.uk/pdbsum/4zgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zgu 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;">
+
-
== 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<ref>PMID:27524203</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4zgu" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Retinol-binding protein|Retinol-binding protein]]
+
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Geiger, J]]
+
[[Category: Homo sapiens]]
-
[[Category: Nossoni, Z]]
+
[[Category: Large Structures]]
-
[[Category: 3d domain swapping human crbpii protein dimerization]]
+
[[Category: Geiger J]]
-
[[Category: Transport protein]]
+
[[Category: Nossoni Z]]

Current revision

Crystal structure of monomer Y60W hCRBPII

PDB ID 4zgu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4zgu"
Personal tools