1epa: Difference between revisions
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[[Image:1epa.gif|left|200px]] | [[Image:1epa.gif|left|200px]] | ||
'''STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1epa |SIZE=350|CAPTION= <scene name='initialview01'>1epa</scene>, resolution 2.1Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EPA is a [ | 1EPA is a [[Single protein]] structure of sequence from [http://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]. | ||
==Reference== | ==Reference== | ||
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:// | 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://www.ncbi.nlm.nih.gov/pubmed/8069623 8069623] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: retinoic acid-binding protein]] | [[Category: retinoic acid-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:38 2008'' | ||
Revision as of 11:58, 20 March 2008
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STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION
OverviewOverview
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 StructureAbout this Structure
1EPA is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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
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