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==NMR SOLUTION STRUCTURE OF HUMAN CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II, 22 STRUCTURES==
<StructureSection load='1blr' size='340' side='right'caption='[[1blr]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1blr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BLR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BLR FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRABP-II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1blr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1blr OCA], [http://pdbe.org/1blr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1blr RCSB], [http://www.ebi.ac.uk/pdbsum/1blr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1blr ProSAT]</span></td></tr>
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== Function ==
[[http://www.uniprot.org/uniprot/RABP2_HUMAN RABP2_HUMAN]] Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bl/1blr_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=1blr ConSurf].
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== Publication Abstract from PubMed ==
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances of apo-CRABPII were established by multinuclear, multidimensional NMR spectroscopy. The solution structure of apo-CRABPII was derived from 2382 experimental NMR restraints using a hybrid distance geometry-simulated annealing protocol. The root-mean-square deviation of the ensemble of 25 refined conformers that represent the structure from the mean coordinate set derived from them was 0.54 +/- 0.18 and 0.92 +/- 0.20 A for the backbone atoms and all heavy atoms, respectively, of all residues except Ala32-Pro39 and Thr57-Glu62, which are in disordered regions. The solution structure of apo-CRABPII is similar to the crystal structure of holo-CRABPII [Kleywegt, G. J., Bergfors, T., Senn, H., Le Motte, P., Gsell, B., Shudo, K., and Jones, T. A. (1994) Structure 2, 1241-1258] except the ligand entrance, which is sufficiently enlarged in the apoprotein to be readily accessible to retinoic acid. The enlargement of the ligand entrance of apo-CRABPII relative to that of holo-CRABPII is due mainly to a concerted conformational change in three structural elements, namely, the second helix, the betaC-betaD loop, and the betaE-betaF loop. Furthermore, the ligand-binding pocket of apo-CRABPII showed evidence of dynamic disorder; among the 21 residues that constitute this pocket, 16 residues had weak or no detectable cross-peaks in the two-dimensional 1H-15N HSQC spectrum recorded under conditions of minimal water saturation or dephasing. Apo-CRABPII is largely monomeric in solution, with no evidence for the dimeric structure shown in the crystal structure of apo-CRABPI which was suggested to be a prerequisite for ligand entry [Thompson, J. R., Bratt, J. M., and Banaszak, L. J. (1995) J. Mol. Biol. 252, 433-446]. Thus, the widening of the ligand entrance required for entry of retinoic acid appears to be a property of monomeric apo-CRABPII.

NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.,Wang L, Li Y, Abildgaard F, Markley JL, Yan H Biochemistry. 1998 Sep 15;37(37):12727-36. PMID:9737849<ref>PMID:9737849</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[CRABP I ( Cellular Retinoic Acid Binding Protein )|CRABP I ( Cellular Retinoic Acid Binding Protein )]]
*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
*[[Gustavo Elberto Epalza Sanchez/Sandbox 1|Gustavo Elberto Epalza Sanchez/Sandbox 1]]
*[[Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)|Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)]]
== References ==
<references/>
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</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Abilddard, F]]
[[Category: Li, Y]]
[[Category: Markely, J]]
[[Category: Wang, L]]
[[Category: Yan, H]]
[[Category: Crabpii]]
[[Category: Transport]]
[[Category: Vitamin some]]