1kgl: Difference between revisions
No edit summary |
No edit summary |
||
| (11 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol== | ||
<StructureSection load='1kgl' size='340' side='right'caption='[[1kgl]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kgl]] 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=1KGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KGL FirstGlance]. <br> | |||
</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=1kgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgl OCA], [https://pdbe.org/1kgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kgl RCSB], [https://www.ebi.ac.uk/pdbsum/1kgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kgl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RET1_RAT RET1_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/kg/1kgl_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=1kgl ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Retinoid-binding proteins play an important role in regulating transport, storage, and metabolism of vitamin A and its derivatives. The solution structure and backbone dynamics of rat cellular retinol-binding protein type I (CRBP) in the apo- and holo-form have been determined and compared using multidimensional high resolution NMR spectroscopy. The global fold of the protein is consistent with the common motif described for members of the intracellular lipid-binding protein family. The most relevant difference between the NMR structure ensembles of apo- and holoCRBP is the higher backbone disorder, in the ligand-free form, of some segments that frame the putative entrance to the ligand-binding site. These comprise alpha-helix II, the subsequent linker to beta-strand B, the hairpin turn between beta-strands C and D, and the betaE-betaF turn. The internal backbone dynamics, obtained from 15N relaxation data (T1, T2, and heteronuclear nuclear Overhauser effect) at two different fields, indicate several regions with significantly higher backbone mobility in the apoprotein, including the betaC-betaD and betaE-betaF turns. Although apoCRBP contains a binding cavity more shielded than that of any other retinoid carrier, conformational flexibility in the portal region may assist retinol uptake. The stiffening of the backbone in the holoprotein guarantees the stability of the complex during retinol transport and suggests that targeted retinol release requires a transiently open state that is likely to be promoted by the acceptor or the local environment. | |||
Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution.,Franzoni L, Lucke C, Perez C, Cavazzini D, Rademacher M, Ludwig C, Spisni A, Rossi GL, Ruterjans H J Biol Chem. 2002 Jun 14;277(24):21983-97. Epub 2002 Apr 4. PMID:11934897<ref>PMID:11934897</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kgl" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Cavazzini D]] | |||
[[Category: Cavazzini | [[Category: Franzoni L]] | ||
[[Category: Franzoni | [[Category: Ludwig C]] | ||
[[Category: Ludwig | [[Category: Luecke C]] | ||
[[Category: Luecke | [[Category: Perez C]] | ||
[[Category: Perez | [[Category: Rademacher M]] | ||
[[Category: Rademacher | [[Category: Rossi GL]] | ||
[[Category: Rossi | [[Category: Rueterjans H]] | ||
[[Category: Rueterjans | [[Category: Spisni A]] | ||
[[Category: Spisni | |||
Latest revision as of 11:41, 22 May 2024
Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinolSolution structure of cellular retinol binding protein type-I in complex with all-trans-retinol
Structural highlights
FunctionRET1_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 PubMedRetinoid-binding proteins play an important role in regulating transport, storage, and metabolism of vitamin A and its derivatives. The solution structure and backbone dynamics of rat cellular retinol-binding protein type I (CRBP) in the apo- and holo-form have been determined and compared using multidimensional high resolution NMR spectroscopy. The global fold of the protein is consistent with the common motif described for members of the intracellular lipid-binding protein family. The most relevant difference between the NMR structure ensembles of apo- and holoCRBP is the higher backbone disorder, in the ligand-free form, of some segments that frame the putative entrance to the ligand-binding site. These comprise alpha-helix II, the subsequent linker to beta-strand B, the hairpin turn between beta-strands C and D, and the betaE-betaF turn. The internal backbone dynamics, obtained from 15N relaxation data (T1, T2, and heteronuclear nuclear Overhauser effect) at two different fields, indicate several regions with significantly higher backbone mobility in the apoprotein, including the betaC-betaD and betaE-betaF turns. Although apoCRBP contains a binding cavity more shielded than that of any other retinoid carrier, conformational flexibility in the portal region may assist retinol uptake. The stiffening of the backbone in the holoprotein guarantees the stability of the complex during retinol transport and suggests that targeted retinol release requires a transiently open state that is likely to be promoted by the acceptor or the local environment. Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution.,Franzoni L, Lucke C, Perez C, Cavazzini D, Rademacher M, Ludwig C, Spisni A, Rossi GL, Ruterjans H J Biol Chem. 2002 Jun 14;277(24):21983-97. Epub 2002 Apr 4. PMID:11934897[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||