1eii
From Proteopedia
(New page: 200px<br /><applet load="1eii" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eii" /> '''NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDI...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1eii.jpg|left|200px]]<br /><applet load="1eii" size=" | + | [[Image:1eii.jpg|left|200px]]<br /><applet load="1eii" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eii" /> | caption="1eii" /> | ||
'''NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II'''<br /> | '''NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure and backbone dynamics of rat holo cellular retinol-binding | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1EII 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:// | + | 1EII 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=1EII OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cistola, D | + | [[Category: Cistola, D P.]] |
| - | [[Category: Kao, J | + | [[Category: Kao, J L.]] |
[[Category: Li, E.]] | [[Category: Li, E.]] | ||
| - | [[Category: Lin, C | + | [[Category: Lin, C L.]] |
[[Category: Lu, J.]] | [[Category: Lu, J.]] | ||
| - | [[Category: Ponder, J | + | [[Category: Ponder, J W.]] |
[[Category: Tang, C.]] | [[Category: Tang, C.]] | ||
[[Category: RTL]] | [[Category: RTL]] | ||
| Line 25: | Line 25: | ||
[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:13 2008'' |
Revision as of 10:28, 21 February 2008
|
NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II
Overview
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.
About this Structure
1EII is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:28:13 2008
