1cbq: Difference between revisions

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[[Image:1cbq.jpg|left|200px]]<br /><applet load="1cbq" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1cbq.jpg|left|200px]]
caption="1cbq, resolution 2.2&Aring;" />
 
'''CRYSTAL STRUCTURE OF CELLULAR RETINOIC-ACID-BINDING PROTEINS I AND II IN COMPLEX WITH ALL-TRANS-RETINOIC ACID AND A SYNTHETIC RETINOID'''<br />
{{Structure
|PDB= 1cbq |SIZE=350|CAPTION= <scene name='initialview01'>1cbq</scene>, resolution 2.2&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=RE9:6-(2,3,4,5,6,7-HEXAHYDRO-2,4,4-TRIMETHYL-1-METYLENEINDEN-2-YL)-3-METHYLHEXA-2,4-DIENOIC ACID'>RE9</scene>
|ACTIVITY=
|GENE= HUMAN CRABP-II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''CRYSTAL STRUCTURE OF CELLULAR RETINOIC-ACID-BINDING PROTEINS I AND II IN COMPLEX WITH ALL-TRANS-RETINOIC ACID AND A SYNTHETIC RETINOID'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1CBQ 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=PO4:'>PO4</scene> and <scene name='pdbligand=RE9:'>RE9</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBQ OCA].  
1CBQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBQ OCA].  


==Reference==
==Reference==
Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid., Kleywegt GJ, Bergfors T, Senn H, Le Motte P, Gsell B, Shudo K, Jones TA, Structure. 1994 Dec 15;2(12):1241-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7704533 7704533]
Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid., Kleywegt GJ, Bergfors T, Senn H, Le Motte P, Gsell B, Shudo K, Jones TA, Structure. 1994 Dec 15;2(12):1241-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7704533 7704533]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: retinoic-acid transport]]
[[Category: retinoic-acid transport]]


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Revision as of 11:22, 20 March 2008

File:1cbq.jpg


PDB ID 1cbq

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: and
Gene: HUMAN CRABP-II (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 StructureAbout this Structure

1CBQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid., Kleywegt GJ, Bergfors T, Senn H, Le Motte P, Gsell B, Shudo K, Jones TA, Structure. 1994 Dec 15;2(12):1241-58. PMID:7704533

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