2frs: Difference between revisions

Revision as of 07:09, 28 July 2008

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File:2frs.png

Template:STRUCTURE 2frs

Crystal structure of the f15w mutant of apo-cellular retinoic acid binding protein type ii at 1.51 angstroms resolutionCrystal structure of the f15w mutant of apo-cellular retinoic acid binding protein type ii at 1.51 angstroms resolution

Template:ABSTRACT PUBMED 16979656

About this StructureAbout this Structure

2FRS is a Single protein structure of sequence from Homo sapiens. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2frs.gif|left|200px]]
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-'''Crystal structure of the f15w mutant of apo-cellular retinoic acid binding protein type ii at 1.51 angstroms resolution'''
+===Crystal structure of the f15w mutant of apo-cellular retinoic acid binding protein type ii at 1.51 angstroms resolution===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16979656}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16979656 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16979656}}
 ==About this Structure==
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 [[Category: Retinoid]]
 [[Category: X-ray]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:14:17 2008''
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