1kgl
From Proteopedia
(New page: 200px<br /><applet load="1kgl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgl" /> '''Solution structure of cellular retinol bindi...) |
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| - | [[Image:1kgl.jpg|left|200px]]<br /><applet load="1kgl" size=" | + | [[Image:1kgl.jpg|left|200px]]<br /><applet load="1kgl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kgl" /> | caption="1kgl" /> | ||
'''Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol'''<br /> | '''Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Retinoid-binding proteins play an important role in regulating transport, storage, and metabolism of vitamin A and its derivatives. The solution | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1KGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with RTL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1KGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=RTL:'>RTL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Perez, C.]] | [[Category: Perez, C.]] | ||
[[Category: Rademacher, M.]] | [[Category: Rademacher, M.]] | ||
| - | [[Category: Rossi, G | + | [[Category: Rossi, G L.]] |
[[Category: Rueterjans, H.]] | [[Category: Rueterjans, H.]] | ||
[[Category: Spisni, A.]] | [[Category: Spisni, A.]] | ||
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[[Category: retinoid carrier]] | [[Category: retinoid carrier]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:59 2008'' |
Revision as of 11:34, 21 February 2008
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Solution structure of cellular retinol binding protein type-I in complex with all-trans-retinol
Overview
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.
About this Structure
1KGL is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
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
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