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New page: left|200px<br /><applet load="1cbi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cbi, resolution 2.7Å" /> '''APO-CELLULAR RETINOIC...
 
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[[Image:1cbi.jpg|left|200px]]<br /><applet load="1cbi" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cbi, resolution 2.7&Aring;" />
'''APO-CELLULAR RETINOIC ACID BINDING PROTEIN I'''<br />


==Overview==
==APO-CELLULAR RETINOIC ACID BINDING PROTEIN I==
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.
<StructureSection load='1cbi' size='340' side='right'caption='[[1cbi]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RABP1_MOUSE RABP1_MOUSE] Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/1cbi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CBI OCA].
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=7563063 7563063]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Banaszak LJ]]
[[Category: Banaszak, L.J.]]
[[Category: Bratt JM]]
[[Category: Bratt, J.M.]]
[[Category: Thompson JR]]
[[Category: Thompson, J.R.]]
[[Category: retinoic-acid transport]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:19:14 2007''

Latest revision as of 06:42, 7 February 2024

APO-CELLULAR RETINOIC ACID BINDING PROTEIN I

1cbi, resolution 2.70Å

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