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| | ==NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II== | | ==NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II== |
| - | <StructureSection load='1eii' size='340' side='right'caption='[[1eii]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | + | <StructureSection load='1eii' size='340' side='right'caption='[[1eii]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1eii]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EII FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1eii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EII FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RTL:RETINOL'>RTL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b4m|1b4m]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RTL:RETINOL'>RTL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eii OCA], [http://pdbe.org/1eii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eii RCSB], [http://www.ebi.ac.uk/pdbsum/1eii PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eii ProSAT]</span></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=1eii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eii OCA], [https://pdbe.org/1eii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eii RCSB], [https://www.ebi.ac.uk/pdbsum/1eii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eii ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RET2_RAT RET2_RAT]] Intracellular transport of retinol. | + | [https://www.uniprot.org/uniprot/RET2_RAT RET2_RAT] Intracellular transport of retinol. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Retinol-binding protein|Retinol-binding protein]] | + | *[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cistola, D P]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Kao, J L]] | + | [[Category: Cistola DP]] |
| - | [[Category: Li, E]] | + | [[Category: Kao JL]] |
| - | [[Category: Lin, C L]] | + | [[Category: Li E]] |
| - | [[Category: Lu, J]] | + | [[Category: Lin CL]] |
| - | [[Category: Ponder, J W]] | + | [[Category: Lu J]] |
| - | [[Category: Tang, C]] | + | [[Category: Ponder JW]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Tang C]] |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Protein-ligand complex]]
| + | |
| - | [[Category: Transport protein]]
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| Structural highlights
Function
RET2_RAT Intracellular transport of retinol.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure and backbone dynamics of rat holo cellular retinol-binding protein II (holo-CRBP II) in solution has been determined by multidimensional NMR. The final structure ensemble was based on 3980 distance and 30 dihedral angle restraints, and was calculated using metric matrix distance geometry with pairwise Gaussian metrization followed by simulated annealing. The average RMS deviation of the backbone atoms for the final 25 structures relative to their mean coordinates is 0.85(+/-0.09) A. Comparison of the solution structure of holo-CRBP II with apo-CRBP II indicates that the protein undergoes conformational changes not previously observed in crystalline CRBP II, affecting residues 28-35 of the helix-turn-helix, residues 37-38 of the subsequent linker, as well as the beta-hairpin C-D, E-F and G-H loops. The bound retinol is completely buried inside the binding cavity and oriented as in the crystal structure. The order parameters derived from the (15)N T(1), T(2) and steady-state NOE parameters show that the backbone dynamics of holo-CRBP II is restricted throughout the polypeptide. The T(2) derived apparent backbone exchange rate and amide (1)H exchange rate both indicate that the microsecond to second timescale conformational exchange occurring in the portal region of the apo form has been suppressed in the holo form.
Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics.,Lu J, Lin CL, Tang C, Ponder JW, Kao JL, Cistola DP, Li E J Mol Biol. 2000 Jul 14;300(3):619-32. PMID:10884357[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lu J, Lin CL, Tang C, Ponder JW, Kao JL, Cistola DP, Li E. Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics. J Mol Biol. 2000 Jul 14;300(3):619-32. PMID:10884357 doi:10.1006/jmbi.2000.3883
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