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==RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA== | ==RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA== | ||
<StructureSection load='1aqb' size='340' side='right' caption='[[1aqb]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='1aqb' size='340' side='right'caption='[[1aqb]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aqb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1aqb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa_domesticus Sus scrofa domesticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQB FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=RTL:RETINOL'>RTL</scene>< | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=RTL:RETINOL'>RTL</scene></td></tr> | ||
<table> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqb OCA], [https://pdbe.org/1aqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aqb RCSB], [https://www.ebi.ac.uk/pdbsum/1aqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aqb ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RET4_PIG RET4_PIG] Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aq/1aqb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aq/1aqb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aqb ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1aqb" 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 == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa domesticus]] | [[Category: Sus scrofa domesticus]] | ||
[[Category: Berni | [[Category: Berni R]] | ||
[[Category: Folli | [[Category: Folli C]] | ||
[[Category: Malpeli | [[Category: Malpeli G]] | ||
[[Category: Marcato | [[Category: Marcato A]] | ||
[[Category: Panzalorto | [[Category: Panzalorto M]] | ||
[[Category: Zanotti | [[Category: Zanotti G]] | ||
Latest revision as of 02:47, 21 November 2024
RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMARETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA
Structural highlights
FunctionRET4_PIG Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of pig plasma retinol-binding protein (RBP) has been determined at 1.65 A resolution. The space group is P212121, with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the asymmetric unit. The structure has been solved using the molecular replacement method and refined with restrained least squares to an R factor of 0.1844 and an Rfree of 0.237 for 18 874 and 1001 independent reflections, respectively. The relatively high resolution structure of pig holoRBP has revealed some new structural details. Moreover, it has provided a description of the binding site for Cd2+, a metal ion which is required for protein crystallization. The hepta-coordination of the RBP-bound cadmium ion involves different residues of two symmetry-related RBP molecules, consistent with the participation of the cation in intermolecular interactions that in turn promote protein crystallization. Structure of pig plasma retinol-binding protein at 1.65 A resolution.,Zanotti G, Panzalorto M, Marcato A, Malpeli G, Folli C, Berni R Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1049-52. PMID:9757135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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