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1fem

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(New page: 200px<br /><applet load="1fem" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fem, resolution 1.9&Aring;" /> '''CRYSTALLOGRAPHIC STUD...)
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[[Image:1fem.gif|left|200px]]<br /><applet load="1fem" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fem, resolution 1.9&Aring;" />
 
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'''CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN'''<br />
 
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==Overview==
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==CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN==
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The three-dimensional structures of complexes between bovine plasma, retinol-binding protein (RBP) and three retinol analogs with different end, groups (fenretinide, all-trans retinoic acid, and axerophthene) have been, determined to 1.8-1.9-A resolution. Their models are very similar to that, of the bovine retinol.RBP complex: the root mean square deviations between, equivalent alpha-carbons in the two proteins range from 0.17 to 0.24 A., The retinoid molecules fit in the beta-barrel cavity assuming the same, conformation of the vitamin, and the substitutions have no consequences on, the overall protein structure. While confirming that an intact hydroxyl, end group is not an absolute requirement for a correct retinoid binding to, RBP, this study has shown the occurrence of conformational changes, although limited, in the rather flexible loop region at the entrance of, the beta-barrel upon fenretinide and retinoic acid binding. These changes, are suitable for accommodating the end groups of the above retinoids., Instead, no such changes have been revealed in RBP complexed with, axerophthene, a retinol analog bearing a hydrogen atom in place of the, hydroxyl end group. The protein conformational changes in the above loop, region, the steric hindrance of bulky end groups of bound retinoids, and, the lack of the retinol hydroxyl group appear to be responsible for the, possible reduced affinity of retinoids for RBP relative to retinol and, at, the same time, for the abolished or reduced affinity of retinoid.RBP, complexes for transthyretin relative to retinol-RBP.
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<StructureSection load='1fem' size='340' side='right'caption='[[1fem]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FEM FirstGlance]. <br>
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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]] 1.9&#8491;</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=REA:RETINOIC+ACID'>REA</scene></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=1fem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fem OCA], [https://pdbe.org/1fem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fem RCSB], [https://www.ebi.ac.uk/pdbsum/1fem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fem ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RET4_BOVIN RET4_BOVIN] 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1fem_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fem ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with REA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FEM OCA].
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*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystallographic studies on complexes between retinoids and plasma retinol-binding protein., Zanotti G, Marcello M, Malpeli G, Folli C, Sartori G, Berni R, J Biol Chem. 1994 Nov 25;269(47):29613-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7961949 7961949]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Berni, R.]]
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[[Category: Berni R]]
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[[Category: Malpeli, G.]]
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[[Category: Malpeli G]]
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[[Category: Marcello, M.]]
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[[Category: Marcello M]]
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[[Category: Sartori, G.]]
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[[Category: Sartori G]]
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[[Category: Zanotti, G.]]
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[[Category: Zanotti G]]
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[[Category: REA]]
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[[Category: transport protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:51:22 2007''
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Current revision

CRYSTALLOGRAPHIC STUDIES ON COMPLEXES BETWEEN RETINOIDS AND PLASMA RETINOL-BINDING PROTEIN

PDB ID 1fem

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