1epb
From Proteopedia
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| - | [[Image:1epb.gif|left|200px]] | + | [[Image:1epb.gif|left|200px]] |
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| - | '''STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1epb |SIZE=350|CAPTION= <scene name='initialview01'>1epb</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=REA:RETINOIC ACID'>REA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''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== | ||
| - | 1EPB is a [ | + | 1EPB 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=1EPB 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 10:58:39 2008'' |
Revision as of 08:58, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION
Overview
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
1EPB is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
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:8069623
Page seeded by OCA on Thu Mar 20 10:58:39 2008
