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1b4m

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NMR STRUCTURE OF APO CELLULAR RETINOL-BINDING PROTEIN II, 24 STRUCTURES

Structural highlights

1b4m is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 dynamics of rat apo-cellular retinol binding protein II (apo-CRBP II) in solution has been determined by multidimensional NMR analysis of uniformly enriched recombinant rat 13C, 15N-apo-CRBP II and 15N-apo-CRBP II. The final ensemble of 24 NMR structures has been calculated from 3274 conformational restraints or 24.4 restraints/residue. The average root-mean-square deviation of the backbone atoms for the final 24 structures relative to their mean structure is 1.06 A. Although the average solution structure is very similar to the crystal structure, it differs at the putative entrance to the binding cavity, which is formed by the helix-turn-helix motif, the betaC-betaD turn and the betaE-betaF turn. The mean coordinates of the main-chain atoms of amino acid residues 28-38 are displaced in the solution structure relative to the crystal structure. The side-chain of F58, located on the betaC-betaD turn, is reoriented such that it interacts with L37 and no longer blocks entry into the ligand-binding pocket. Residues 28-35, which form the second helix of the helix-turn-helix motif in the crystal structure, do not exhibit a helical conformation in the solution structure. The solution structure of apo-CRBP II exhibits discrete regions of backbone disorder which are most pronounced at residues 28-32, 37-38 and 73-76 in the betaE-betaF turn as evaluated by the consensus chemical shift index, the root-mean-square deviation, amide 1H exchange rates and 15N relaxation studies. These studies indicate that fluctuations in protein conformation occur on the microseconds to ms time-scale in these regions of the protein. Some of these exchange processes can be directly observed in the three-dimensional 15N-resolved NOESY spectrum. These results suggest that in solution, apo-CRBP II undergoes conformational changes on the microseconds to ms time-scale which result in increased access to the binding cavity.

The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure.,Lu J, Lin CL, Tang C, Ponder JW, Kao JL, Cistola DP, Li E J Mol Biol. 1999 Mar 5;286(4):1179-95. PMID:10047490^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lu J, Lin CL, Tang C, Ponder JW, Kao JL, Cistola DP, Li E. The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure. J Mol Biol. 1999 Mar 5;286(4):1179-95. PMID:10047490 doi:10.1006/jmbi.1999.2544

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b4m"

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURE OF APO CELLULAR RETINOL-BINDING PROTEIN II, 24 STRUCTURES==
-<StructureSection load='1b4m' size='340' side='right' caption='[[1b4m]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''>
+<StructureSection load='1b4m' size='340' side='right'caption='[[1b4m]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1b4m]] 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=1B4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B4M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1b4m]] 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=1B4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B4M FirstGlance]. <br>
-</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=1b4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4m OCA], [http://pdbe.org/1b4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b4m RCSB], [http://www.ebi.ac.uk/pdbsum/1b4m PDBsum]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4m OCA], [https://pdbe.org/1b4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b4m RCSB], [https://www.ebi.ac.uk/pdbsum/1b4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b4m ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[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/b4/1b4m_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b4/1b4m_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1b4m ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 30: @@
 ==See Also==
-*[[Retinol-binding protein|Retinol-binding protein]]
+*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Cistola, D P]]
+[[Category: Rattus norvegicus]]
-[[Category: Kao, J L.F]]
+[[Category: Cistola DP]]
-[[Category: Li, E]]
+[[Category: Kao JLF]]
-[[Category: Lin, C L]]
+[[Category: Li E]]
-[[Category: Lu, J]]
+[[Category: Lin C-L]]
-[[Category: Ponder, J W]]
+[[Category: Lu J]]
-[[Category: Tang, C]]
+[[Category: Ponder JW]]
-[[Category: Cellular retinol-binding protein]]
+[[Category: Tang C]]
-[[Category: Crbp ii]]
-[[Category: Lipid transport]]
-[[Category: Lipid-binding protein]]
-[[Category: Retinol transport]]

1b4m

From Proteopedia

Current revision

NMR STRUCTURE OF APO CELLULAR RETINOL-BINDING PROTEIN II, 24 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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