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New page: left|200px<br /><applet load="1epa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1epa, resolution 2.1Å" /> '''STRUCTURE OF THE EPID...
 
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[[Image:1epa.gif|left|200px]]<br /><applet load="1epa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1epa, resolution 2.1&Aring;" />
'''STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION'''<br />


==Overview==
==STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION==
BACKGROUND: Androgen-dependent proteins in the lumen of the epididymis are, required for sperm maturation. One of these is a retinoic acid binding, protein, E-RABP, which binds both all-trans and 9-cis retinoic acid. The, other retinoid-binding proteins whose structures are known do not bind, 9-cis retinoids. RESULTS: We describe the X-ray structure determination of, E-RABP with and without bound ligand. The ligand binds deep in the, beta-barrel of the protein, the beta-ionone ring innermost. The binding, site, like the ligand, is amphipathic and the deepest part of the cavity, is formed by a ring of aromatic amino acids. The isoprene tail of, all-trans retinoic acid is bound in a folded conformation which resembles, that of the 9-cis isomer. CONCLUSION: E-RABP achieves high-affinity, binding of both all-trans and 9-cis isomers of retinoic acid by forcing, the all-trans form to bind in a folded conformation. The RAR family of, nuclear receptors for retinoic acid also binds both isomers, and their, binding sites may therefore be similar.
<StructureSection load='1epa' size='340' side='right'caption='[[1epa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1epa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPA 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]] 2.1&#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=1epa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epa OCA], [https://pdbe.org/1epa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1epa RCSB], [https://www.ebi.ac.uk/pdbsum/1epa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1epa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LCN5_RAT LCN5_RAT] Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 9-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation.
== 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/ep/1epa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1epa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Androgen-dependent proteins in the lumen of the epididymis are required for sperm maturation. One of these is a retinoic acid binding protein, E-RABP, which binds both all-trans and 9-cis retinoic acid. The other retinoid-binding proteins whose structures are known do not bind 9-cis retinoids. RESULTS: We describe the X-ray structure determination of E-RABP with and without bound ligand. The ligand binds deep in the beta-barrel of the protein, the beta-ionone ring innermost. The binding site, like the ligand, is amphipathic and the deepest part of the cavity is formed by a ring of aromatic amino acids. The isoprene tail of all-trans retinoic acid is bound in a folded conformation which resembles that of the 9-cis isomer. CONCLUSION: E-RABP achieves high-affinity binding of both all-trans and 9-cis isomers of retinoic acid by forcing the all-trans form to bind in a folded conformation. The RAR family of nuclear receptors for retinoic acid also binds both isomers, and their binding sites may therefore be similar.


==About this Structure==
Structure of the epididymal retinoic acid binding protein at 2.1 A resolution.,Newcomer ME Structure. 1993 Sep 15;1(1):7-18. PMID:8069623<ref>PMID:8069623</ref>
1EPA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EPA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of the epididymal retinoic acid binding protein at 2.1 A resolution., Newcomer ME, Structure. 1993 Sep 15;1(1):7-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8069623 8069623]
</div>
<div class="pdbe-citations 1epa" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Newcomer ME]]
[[Category: Newcomer, M.E.]]
[[Category: retinoic acid-binding protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:11:53 2007''

Latest revision as of 06:34, 30 October 2024

STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION

1epa, resolution 2.10Å

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