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[[Image:1ggl.gif|left|200px]]
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{{STRUCTURE_1ggl|  PDB=1ggl  |  SCENE=  }}
'''HUMAN CELLULAR RETINOL BINDING PROTEIN III'''


==HUMAN CELLULAR RETINOL BINDING PROTEIN III==
<StructureSection load='1ggl' size='340' side='right'caption='[[1ggl]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ggl]] is a 2 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=1GGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GGL 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]] 2.31&#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=1ggl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggl OCA], [https://pdbe.org/1ggl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ggl RCSB], [https://www.ebi.ac.uk/pdbsum/1ggl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RET5_HUMAN RET5_HUMAN] Intracellular transport of retinol.<ref>PMID:11274389</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/1ggl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1ggl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two cellular retinol-binding proteins (CRBP I and II) with distinct tissue distributions and retinoid-binding properties have been recognized thus far in mammals. Here, we report the identification of a human retinol-binding protein resembling type I (55.6% identity) and type II (49.6% identity) CRBPs, but with a unique H residue in the retinoid-binding site and a distinctively different tissue distribution. Additionally, this binding protein (CRBP III) exhibits a remarkable sequence identity (62.2%) with the recently identified iota-crystallin/CRBP of the diurnal gecko Lygodactylus picturatus [Werten, P. J. L., Roll, B., van Alten, D. M. F. &amp; de Jong, W. W. (2000) Proc. Natl. Acad. Sci. USA 97, 3282-3287 (First Published March 21, 2000; 10.1073/pnas.050500597)]. CRBP III and all-trans-retinol form a complex (K(d) approximately 60 nM), the absorption spectrum of which is characterized by the peculiar fine structure typical of the spectra of holo-CRBP I and II. As revealed by a 2.3-A x-ray molecular model of apo-CRBP III, the amino acid residues that line the retinol-binding site in CRBP I and II are positioned nearly identically in the structure of CRBP III. At variance with the human CRBP I and II mRNAs, which are most abundant in ovary and intestine, respectively, the CRBP III mRNA is expressed at the highest levels in kidney and liver thus suggesting a prominent role for human CRBP III as an intracellular mediator of retinol metabolism in these tissues.


==Overview==
Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein.,Folli C, Calderone V, Ottonello S, Bolchi A, Zanotti G, Stoppini M, Berni R Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3710-5. PMID:11274389<ref>PMID:11274389</ref>
Two cellular retinol-binding proteins (CRBP I and II) with distinct tissue distributions and retinoid-binding properties have been recognized thus far in mammals. Here, we report the identification of a human retinol-binding protein resembling type I (55.6% identity) and type II (49.6% identity) CRBPs, but with a unique H residue in the retinoid-binding site and a distinctively different tissue distribution. Additionally, this binding protein (CRBP III) exhibits a remarkable sequence identity (62.2%) with the recently identified iota-crystallin/CRBP of the diurnal gecko Lygodactylus picturatus [Werten, P. J. L., Roll, B., van Alten, D. M. F. &amp; de Jong, W. W. (2000) Proc. Natl. Acad. Sci. USA 97, 3282-3287 (First Published March 21, 2000; 10.1073/pnas.050500597)]. CRBP III and all-trans-retinol form a complex (K(d) approximately 60 nM), the absorption spectrum of which is characterized by the peculiar fine structure typical of the spectra of holo-CRBP I and II. As revealed by a 2.3-A x-ray molecular model of apo-CRBP III, the amino acid residues that line the retinol-binding site in CRBP I and II are positioned nearly identically in the structure of CRBP III. At variance with the human CRBP I and II mRNAs, which are most abundant in ovary and intestine, respectively, the CRBP III mRNA is expressed at the highest levels in kidney and liver thus suggesting a prominent role for human CRBP III as an intracellular mediator of retinol metabolism in these tissues.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1GGL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGL OCA].
</div>
<div class="pdbe-citations 1ggl" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein., Folli C, Calderone V, Ottonello S, Bolchi A, Zanotti G, Stoppini M, Berni R, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3710-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11274389 11274389]
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berni, R.]]
[[Category: Berni R]]
[[Category: Bolchi, A.]]
[[Category: Bolchi A]]
[[Category: Calderone, V.]]
[[Category: Calderone V]]
[[Category: Folli, C.]]
[[Category: Folli C]]
[[Category: Ottonello, S.]]
[[Category: Ottonello S]]
[[Category: Stoppini, M.]]
[[Category: Stoppini M]]
[[Category: Zanotti, G.]]
[[Category: Zanotti G]]
[[Category: Carrier]]
[[Category: Retinol binding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:32:08 2008''