1fd0

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(New page: 200px<br /> <applet load="1fd0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fd0, resolution 1.38&Aring;" /> '''ISOTYPE SELECTIVITY...)
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[[Image:1fd0.gif|left|200px]]<br />
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[[Image:1fd0.gif|left|200px]]<br /><applet load="1fd0" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1fd0" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1fd0, resolution 1.38&Aring;" />
caption="1fd0, resolution 1.38&Aring;" />
'''ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254'''<br />
'''ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254'''<br />
==Overview==
==Overview==
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Hydrogen bonds between polarized atoms play a crucial role in protein, interactions and are often used in drug design, which usually neglects the, potential of C-H...O hydrogen bonds. The 1.4 A resolution crystal, structure of the ligand binding domain of the retinoic acid receptor, RARgamma complexed with the retinoid SR11254 reveals several types of, C-H...O hydrogen bonds. A striking example is the hydroxyl group of the, ligand that acts as an H bond donor and acceptor, leading to a synergy, between classical and C-H...O hydrogen bonds. This interaction introduces, both specificity and affinity within the hydrophobic ligand pocket. The, similarity of intraprotein and protein-ligand C-H...O interactions, suggests that such bonds should be considered in rational drug design, approaches.
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Hydrogen bonds between polarized atoms play a crucial role in protein interactions and are often used in drug design, which usually neglects the potential of C-H...O hydrogen bonds. The 1.4 A resolution crystal structure of the ligand binding domain of the retinoic acid receptor RARgamma complexed with the retinoid SR11254 reveals several types of C-H...O hydrogen bonds. A striking example is the hydroxyl group of the ligand that acts as an H bond donor and acceptor, leading to a synergy between classical and C-H...O hydrogen bonds. This interaction introduces both specificity and affinity within the hydrophobic ligand pocket. The similarity of intraprotein and protein-ligand C-H...O interactions suggests that such bonds should be considered in rational drug design approaches.
==About this Structure==
==About this Structure==
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1FD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with 254 and LMU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FD0 OCA].
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1FD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=254:'>254</scene> and <scene name='pdbligand=LMU:'>LMU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD0 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Klaholz, B.P.]]
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[[Category: Klaholz, B P.]]
[[Category: Moras, D.]]
[[Category: Moras, D.]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: 254]]
[[Category: 254]]
[[Category: LMU]]
[[Category: LMU]]
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:51:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:25 2008''

Revision as of 10:37, 21 February 2008


1fd0, resolution 1.38Å

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ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254

Overview

Hydrogen bonds between polarized atoms play a crucial role in protein interactions and are often used in drug design, which usually neglects the potential of C-H...O hydrogen bonds. The 1.4 A resolution crystal structure of the ligand binding domain of the retinoic acid receptor RARgamma complexed with the retinoid SR11254 reveals several types of C-H...O hydrogen bonds. A striking example is the hydroxyl group of the ligand that acts as an H bond donor and acceptor, leading to a synergy between classical and C-H...O hydrogen bonds. This interaction introduces both specificity and affinity within the hydrophobic ligand pocket. The similarity of intraprotein and protein-ligand C-H...O interactions suggests that such bonds should be considered in rational drug design approaches.

About this Structure

1FD0 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

C-H...O hydrogen bonds in the nuclear receptor RARgamma--a potential tool for drug selectivity., Klaholz B, Moras D, Structure. 2002 Sep;10(9):1197-204. PMID:12220491

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