1fd0: Difference between revisions

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12220491}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12220491 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural genomic]]

[[Category: Structural proteomics in europe]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Apr 13 08~~:06:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:04:18 2008''

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-[[Image:1fd0.gif|left|200px]]
+{{Seed}}
+[[Image:1fd0.png|left|200px]]
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 {{STRUCTURE_1fd0|  PDB=1fd0  |  SCENE=  }}
-'''ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12220491}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12220491 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12220491}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Structural genomic]]
 [[Category: Structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:06:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:04:18 2008''