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1brq

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(New page: 200px<br /> <applet load="1brq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1brq, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1brq.gif|left|200px]]<br />
 
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<applet load="1brq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1brq, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE TRIGONAL FORM OF HUMAN PLASMA RETINOL-BINDING PROTEIN AT 2.5 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE TRIGONAL FORM OF HUMAN PLASMA RETINOL-BINDING PROTEIN AT 2.5 ANGSTROMS RESOLUTION==
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The three-dimensional structures of the liganded and unliganded forms of, human plasma retinol binding protein (RBP) in the trigonal crystal form, have been solved at 2.5 A resolution. The final model of RBP complexed, with retinol (holoRBP, space group R3, a = b = 104.0 A, c = 74.4 A) has a, crystallographic R factor of 0.176 for 9652 reflections. The unliganded, form, obtained through a purification procedure which included steps based, on hydrophobic interaction chromatography, crystallized isomorphously with, holoRBP and its structure has been refined to an R factor of 0.190 for, 9614 reflections. The structure of the trigonal holo protein is quite, similar to that of the orthorhombic form: the root-mean-square deviation, of all the equivalent alpha-carbons in the two chains is 0.53 A. The, structural comparison between the liganded and unliganded forms of RBP in, the crystal did not reveal gross conformational changes. The most, significant difference between the two forms of the protein is a, conformational change involving residues from 34 to 37. In this region, the movements of side-chains of Leu35 and Phe36 are most noticeable. In, particular, in the unliganded form the side-chain ring of the latter, residue is in the place previously occupied by the alcoholic moiety of, retinol. Our data are consistent with a model in which a region comprising, these residues and at least part of the opening of the beta-barrel is, involved in the recognition between RBP and transthyretin. In the case of, the unliganded form, the central cavity, that is occupied by the vitamin, in the two human crystalline holoRBPs, is filled by electron density that, at the present resolution, we interpret as solvent.
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<StructureSection load='1brq' size='340' side='right'caption='[[1brq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1brq]] 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=1BRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRQ 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]] 2.5&#8491;</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=1brq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brq OCA], [https://pdbe.org/1brq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brq RCSB], [https://www.ebi.ac.uk/pdbsum/1brq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brq ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/RET4_HUMAN RET4_HUMAN] Defects in RBP4 are a cause of retinol-binding protein deficiency (RBP deficiency) [MIM:[https://omim.org/entry/180250 180250]. This condition causes night vision problems. It produces a typical 'fundus xerophthalmicus', featuring a progressed atrophy of the retinal pigment epithelium.
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== Function ==
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[https://www.uniprot.org/uniprot/RET4_HUMAN RET4_HUMAN] 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/br/1brq_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=1brq ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Retinol binding protein, deficiency of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=180250 180250]]
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*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
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__TOC__
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==About this Structure==
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</StructureSection>
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1BRQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRQ OCA].
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==Reference==
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Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 A resolution., Zanotti G, Ottonello S, Berni R, Monaco HL, J Mol Biol. 1993 Mar 20;230(2):613-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8464067 8464067]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Monaco, H.L.]]
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[[Category: Monaco HL]]
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[[Category: Zanotti, G.]]
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[[Category: Zanotti G]]
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[[Category: retinol transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:13:59 2007''
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Current revision

CRYSTAL STRUCTURE OF THE TRIGONAL FORM OF HUMAN PLASMA RETINOL-BINDING PROTEIN AT 2.5 ANGSTROMS RESOLUTION

PDB ID 1brq

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