1eii: Difference between revisions

Revision as of 00:46, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1eii.png

Template:STRUCTURE 1eii

NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN IINMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II

Template:ABSTRACT PUBMED 10884357

About this StructureAbout this Structure

1EII is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

ReferenceReference

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

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OCA

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-'''NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II'''
+===NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10884357}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10884357 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10884357}}
 ==About this Structure==
-EII is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EII OCA].
+EII is a [[Single protein]] structure of sequence from [http://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].
 ==Reference==
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 [[Category: Helix-turn-helix]]
 [[Category: Protein-ligand complex]]
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