1epa: Difference between revisions

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[[Image:1epa.gif|left|200px]]<br /><applet load="1epa" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1epa.gif|left|200px]]<br /><applet load="1epa" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1epa, resolution 2.1Å" />

'''STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION'''<br />

==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.

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==

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].

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://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPA OCA].

==Reference==

Line 13:

[[Category: Rattus norvegicus]]

[[Category: Single protein]]

[[Category: Newcomer, M.E.]]

[[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~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:08 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1epa.gif|left|200px]]<br /><applet load="1epa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1epa.gif|left|200px]]<br /><applet load="1epa" size="350" 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==
-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.
+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==
-EPA 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].
+EPA 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPA OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Newcomer, M.E.]]
+[[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''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:08 2008''