2fr3
From Proteopedia
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|PDB= 2fr3 |SIZE=350|CAPTION= <scene name='initialview01'>2fr3</scene>, resolution 1.48Å | |PDB= 2fr3 |SIZE=350|CAPTION= <scene name='initialview01'>2fr3</scene>, resolution 1.48Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CRABP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CRABP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2fs7|2FS7]], [[2frs|2FRS]], [[2fru|2FRU]], [[2fs6|2FS6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fr3 OCA], [http://www.ebi.ac.uk/pdbsum/2fr3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fr3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Geiger, J H.]] | [[Category: Geiger, J H.]] | ||
[[Category: Vaezeslami, S.]] | [[Category: Vaezeslami, S.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: REA]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: crabpii]] | [[Category: crabpii]] | ||
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[[Category: x-ray]] | [[Category: x-ray]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:06:38 2008'' |
Revision as of 00:06, 31 March 2008
| |||||||
| , resolution 1.48Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | CRABP2 (Homo sapiens) | ||||||
| Related: | 2FS7, 2FRS, 2FRU, 2FS6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 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.
About this Structure
2FR3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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