1cbs: Difference between revisions

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[[Image:1cbs.gif|left|200px]]<br />

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

<applet load="1cbs" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1cbs, resolution 1.8Å" />

'''CRYSTAL STRUCTURE OF CELLULAR RETINOIC-ACID-BINDING PROTEINS I AND II IN COMPLEX WITH ALL-TRANS-RETINOIC ACID AND A SYNTHETIC RETINOID'''<br />

==Overview==

BACKGROUND: Retinoic acid (RA) plays a fundamental role in diverse, cellular activities. Cellular RA binding proteins (CRABPs) are thought to, act by modulating the amount of RA available to nuclear RA receptors., CRABPs and cellular retinol-binding proteins (CRBPs) share a unique fold, of two orthogonal beta-sheets that encapsulate their ligands. It has been, suggested that a trio of residues are the prime determinants defining the, high specificity of CRBPs and CRABPs for their physiological ligands., RESULTS: Bovine/murine CRABP I and human CRABP II have been crystallized, in complex with their natural ligand, all-trans-RA. Human CRABP II has, also been crystallized in complex with a synthetic retinoid, 'compound, 19'. Their structures have been determined and refined at resolutions of, 2.9 A, 1.8 A and 2.2 A, respectively. CONCLUSIONS: The retinoid-binding, site in CRABPs differs significantly from that observed in CRBP., Structural changes in three juxtaposed areas of the protein create a new, displaced binding site for RA. The carboxylate of the ligand interacts, with the expected trio of residues (Arg132, Tyr134 and Arg111; CRABP II, numbering). The RA ligand is almost flat with the beta-ionone ring showing, a significant deviation (-33 degrees) from a cis conformation relative to, the isoprene tail. The edge atoms of the beta-ionone ring are accessible, to solvent in a suitable orientation for presentation to metabolizing, enzymes. The bulkier synthetic retinoid causes small conformational, changes in the protein structure.

BACKGROUND: Retinoic acid (RA) plays a fundamental role in diverse cellular activities. Cellular RA binding proteins (CRABPs) are thought to act by modulating the amount of RA available to nuclear RA receptors. CRABPs and cellular retinol-binding proteins (CRBPs) share a unique fold of two orthogonal beta-sheets that encapsulate their ligands. It has been suggested that a trio of residues are the prime determinants defining the high specificity of CRBPs and CRABPs for their physiological ligands. RESULTS: Bovine/murine CRABP I and human CRABP II have been crystallized in complex with their natural ligand, all-trans-RA. Human CRABP II has also been crystallized in complex with a synthetic retinoid, 'compound 19'. Their structures have been determined and refined at resolutions of 2.9 A, 1.8 A and 2.2 A, respectively. CONCLUSIONS: The retinoid-binding site in CRABPs differs significantly from that observed in CRBP. Structural changes in three juxtaposed areas of the protein create a new, displaced binding site for RA. The carboxylate of the ligand interacts with the expected trio of residues (Arg132, Tyr134 and Arg111; CRABP II numbering). The RA ligand is almost flat with the beta-ionone ring showing a significant deviation (-33 degrees) from a cis conformation relative to the isoprene tail. The edge atoms of the beta-ionone ring are accessible to solvent in a suitable orientation for presentation to metabolizing enzymes. The bulkier synthetic retinoid causes small conformational changes in the protein structure.

==About this Structure==

1CBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with REA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CBS OCA].

1CBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=REA:'>REA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBS OCA].

==Reference==

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Line 14:

[[Category: Single protein]]

[[Category: Bergfors, T.]]

[[Category: Jones, T.A.]]

[[Category: Jones, T A.]]

[[Category: Kleywegt, G.J.]]

[[Category: Kleywegt, G J.]]

[[Category: REA]]

[[Category: retinoic-acid transport]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:20:~~00 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:26 2008''

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-[[Image:1cbs.gif|left|200px]]<br />
+[[Image:1cbs.gif|left|200px]]<br /><applet load="1cbs" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1cbs" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1cbs, resolution 1.8&Aring;" />
 '''CRYSTAL STRUCTURE OF CELLULAR RETINOIC-ACID-BINDING PROTEINS I AND II IN COMPLEX WITH ALL-TRANS-RETINOIC ACID AND A SYNTHETIC RETINOID'''<br />
 ==Overview==
-BACKGROUND: Retinoic acid (RA) plays a fundamental role in diverse, cellular activities. Cellular RA binding proteins (CRABPs) are thought to, act by modulating the amount of RA available to nuclear RA receptors., CRABPs and cellular retinol-binding proteins (CRBPs) share a unique fold, of two orthogonal beta-sheets that encapsulate their ligands. It has been, suggested that a trio of residues are the prime determinants defining the, high specificity of CRBPs and CRABPs for their physiological ligands., RESULTS: Bovine/murine CRABP I and human CRABP II have been crystallized, in complex with their natural ligand, all-trans-RA. Human CRABP II has, also been crystallized in complex with a synthetic retinoid, 'compound, 19'. Their structures have been determined and refined at resolutions of, 2.9 A, 1.8 A and 2.2 A, respectively. CONCLUSIONS: The retinoid-binding, site in CRABPs differs significantly from that observed in CRBP., Structural changes in three juxtaposed areas of the protein create a new, displaced binding site for RA. The carboxylate of the ligand interacts, with the expected trio of residues (Arg132, Tyr134 and Arg111; CRABP II, numbering). The RA ligand is almost flat with the beta-ionone ring showing, a significant deviation (-33 degrees) from a cis conformation relative to, the isoprene tail. The edge atoms of the beta-ionone ring are accessible, to solvent in a suitable orientation for presentation to metabolizing, enzymes. The bulkier synthetic retinoid causes small conformational, changes in the protein structure.
+BACKGROUND: Retinoic acid (RA) plays a fundamental role in diverse cellular activities. Cellular RA binding proteins (CRABPs) are thought to act by modulating the amount of RA available to nuclear RA receptors. CRABPs and cellular retinol-binding proteins (CRBPs) share a unique fold of two orthogonal beta-sheets that encapsulate their ligands. It has been suggested that a trio of residues are the prime determinants defining the high specificity of CRBPs and CRABPs for their physiological ligands. RESULTS: Bovine/murine CRABP I and human CRABP II have been crystallized in complex with their natural ligand, all-trans-RA. Human CRABP II has also been crystallized in complex with a synthetic retinoid, 'compound 19'. Their structures have been determined and refined at resolutions of 2.9 A, 1.8 A and 2.2 A, respectively. CONCLUSIONS: The retinoid-binding site in CRABPs differs significantly from that observed in CRBP. Structural changes in three juxtaposed areas of the protein create a new, displaced binding site for RA. The carboxylate of the ligand interacts with the expected trio of residues (Arg132, Tyr134 and Arg111; CRABP II numbering). The RA ligand is almost flat with the beta-ionone ring showing a significant deviation (-33 degrees) from a cis conformation relative to the isoprene tail. The edge atoms of the beta-ionone ring are accessible to solvent in a suitable orientation for presentation to metabolizing enzymes. The bulkier synthetic retinoid causes small conformational changes in the protein structure.
 ==About this Structure==
-CBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with REA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CBS OCA].
+CBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=REA:'>REA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBS OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Bergfors, T.]]
-[[Category: Jones, T.A.]]
+[[Category: Jones, T A.]]
-[[Category: Kleywegt, G.J.]]
+[[Category: Kleywegt, G J.]]
 [[Category: REA]]
 [[Category: retinoic-acid transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:20:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:26 2008''