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1cbi

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[[Image:1cbi.jpg|left|200px]]
 
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{{Structure
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==APO-CELLULAR RETINOIC ACID BINDING PROTEIN I==
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|PDB= 1cbi |SIZE=350|CAPTION= <scene name='initialview01'>1cbi</scene>, resolution 2.7&Aring;
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<StructureSection load='1cbi' size='340' side='right'caption='[[1cbi]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1cbi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CBI FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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|GENE= MOUSE CRABPI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbi OCA], [https://pdbe.org/1cbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cbi RCSB], [https://www.ebi.ac.uk/pdbsum/1cbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cbi ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cbi OCA], [http://www.ebi.ac.uk/pdbsum/1cbi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cbi RCSB]</span>
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[https://www.uniprot.org/uniprot/RABP1_MOUSE RABP1_MOUSE] Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/1cbi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cbi ConSurf].
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<div style="clear:both"></div>
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'''APO-CELLULAR RETINOIC ACID BINDING PROTEIN I'''
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==See Also==
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*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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A recombinant form of murine apo-cellular retinoic acid binding protein I (apo-CRABPI) has been purified and crystallized at pH 5.0, and the crystal structure has been refined to an R-factor of 19.6% at a resolution of 2.7 A. CRABPI binds all-trans retinoic acid and some retinoic acid metabolites with nanomolar affinities. Coordinates of the holo form of CRABP were not available during the early stages of the study, and in spite of numerous homologs of known structure, phases were not obtainable through molecular replacement. Instead, an interpretable electron density map was obtained by multiple isomorphous replacement methods after improvement of the heavy-atom parameters with density modified trial phases. Two molecules of apo-CRABPI occupy the P3121 asymmetric unit and are related by pseudo 2-fold rotational symmetry. Unique conformational differences are apparent between the two molecules. In all of the family members studied to date, there is a lack of hydrogen bonds between two of the component beta-strands resulting in a gap in the interstand hydrogen bonding pattern. In the crystallographic dimer described here, a continuous intermolecular beta-sheet is formed by using this gap region. This is possible because of an 8 A outward maximum displacement of the tight turn between the third and fourth beta-strands on one of the molecules. The result is a double beta-barrel containing two apo-CRABPI molecules with a more open, ligand-accessible binding cavity, which has not been observed in other structures of a family of proteins that bind hydrophobic ligands.
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[[Category: Large Structures]]
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==About this Structure==
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1CBI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBI OCA].
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==Reference==
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Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet., Thompson JR, Bratt JM, Banaszak LJ, J Mol Biol. 1995 Sep 29;252(4):433-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7563063 7563063]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Banaszak LJ]]
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[[Category: Banaszak, L J.]]
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[[Category: Bratt JM]]
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[[Category: Bratt, J M.]]
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[[Category: Thompson JR]]
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[[Category: Thompson, J R.]]
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[[Category: retinoic-acid transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:24 2008''
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Current revision

APO-CELLULAR RETINOIC ACID BINDING PROTEIN I

PDB ID 1cbi

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