2fr3: Difference between revisions
New page: left|200px<br /> <applet load="2fr3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fr3, resolution 1.48Å" /> '''Crystal Structure o... |
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[[Image:2fr3.gif|left|200px]]<br /> | [[Image:2fr3.gif|left|200px]]<br /><applet load="2fr3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 Angstroms Resolution'''<br /> | '''Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 Angstroms Resolution'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2FR3 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 ACT and REA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2FR3 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=ACT:'>ACT</scene> and <scene name='pdbligand=REA:'>REA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FR3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: x-ray]] | [[Category: x-ray]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:26:02 2008'' | ||
Revision as of 18:26, 15 February 2008
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Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 Angstroms Resolution
OverviewOverview
CRABPII is a small, cytosolic protein that solubilizes and transfers, retinoic acid (RA) to the nucleus while also enhancing its transcriptional, activity. We have determined the first high-resolution structure of, apo-wild type (WT) CRABPII at 1.35 A. Using three different data sets, collected on apo-WT CRABPII we have shown that apo- and holo-CRABPII share, very similar structures. Binding of RA appears to increase the overall, rigidity of the structure, although the induced structural changes are not, as pronounced as previously thought. The enhanced structural rigidity may, be an important determinant for the enhanced nuclear localization of the, RA-bound protein. Comparison of our apo-WT with a mutant apo-CRABPII, structure shows that mutation of Arg111, a conserved residue of CRABPII, and a key residue in RA binding, causes structural changes in the, molecule. We further investigated the structural importance of conserved, residues by determining the structure of the F15W mutant CRABPII, (F15W-CRABPII). Our structures also demonstrate structural changes induced, by crystal packing and show that a crystal can harbor demonstrative, structural differences in the asymmetric unit.
About this StructureAbout this Structure
2FR3 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation., Vaezeslami S, Mathes E, Vasileiou C, Borhan B, Geiger JH, J Mol Biol. 2006 Oct 27;363(3):687-701. Epub 2006 Aug 26. PMID:16979656
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