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1epa
From Proteopedia
(Difference between revisions)
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<StructureSection load='1epa' size='340' side='right'caption='[[1epa]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1epa' size='340' side='right'caption='[[1epa]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1epa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1epa ConSurf]. | </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="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. | ||
| - | |||
| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1epa" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]] | *[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Rattus norvegicus]] |
| - | [[Category: | + | [[Category: Newcomer ME]] |
Current revision
STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION
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