This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1epa

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:02, 6 September 2017

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

Structural highlights

1epa is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Newcomer ME. Structure of the epididymal retinoic acid binding protein at 2.1 A resolution. Structure. 1993 Sep 15;1(1):7-18. PMID:8069623

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1epa"

Categories: Newcomer, M E | Retinoic acid-binding protein

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION==
 <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 [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EPA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1epa]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1epa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epa OCA], [http://pdbe.org/1epa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1epa RCSB], [http://www.ebi.ac.uk/pdbsum/1epa PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1epa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epa OCA], [http://pdbe.org/1epa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1epa RCSB], [http://www.ebi.ac.uk/pdbsum/1epa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1epa ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
     <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/chain_selection.php?pdb_ID=2ata 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="background-color:#fffaf0;">
@@ Line 33: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Newcomer, M E]]
 [[Category: Retinoic acid-binding protein]]

1epa

From Proteopedia

Revision as of 04:02, 6 September 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox