2hwc: Difference between revisions

Revision as of 03:06, 29 July 2008

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File:2hwc.png

Template:STRUCTURE 2hwc

A COMPARISON OF THE ANTI-RHINOVIRAL DRUG BINDING POCKET IN HRV14 AND HRV1AA COMPARISON OF THE ANTI-RHINOVIRAL DRUG BINDING POCKET IN HRV14 AND HRV1A

Template:ABSTRACT PUBMED 8383771

About this StructureAbout this Structure

2HWC is a Protein complex structure of sequences from Human rhinovirus 14. Full crystallographic information is available from OCA.

ReferenceReference

A comparison of the anti-rhinoviral drug binding pocket in HRV14 and HRV1A., Kim KH, Willingmann P, Gong ZX, Kremer MJ, Chapman MS, Minor I, Oliveira MA, Rossmann MG, Andries K, Diana GD, et al., J Mol Biol. 1993 Mar 5;230(1):206-27. PMID:8383771

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OCA

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 {{STRUCTURE_2hwc|  PDB=2hwc  |  SCENE=  }}
-'''A COMPARISON OF THE ANTI-RHINOVIRAL DRUG BINDING POCKET IN HRV14 AND HRV1A'''
+===A COMPARISON OF THE ANTI-RHINOVIRAL DRUG BINDING POCKET IN HRV14 AND HRV1A===
-==Overview==
+<!--
-The three-dimensional structures of two human rhinovirus serotypes (HRV14 and HRV1A) are compared when complexed with various antiviral agents. Although these agents all bind into the same hydrophobic pocket, the exact viral-drug interactions differ. In the absence of drugs, the pocket is occupied by a fatty acid in HRV1A, but is empty in HRV14 except for two water molecules. The conformation of each drug is dependent upon the shape of the hydrophobic pocket. In HRV14 the major residues determining the shape of the binding site are Y1128, P1174 and M1224, corresponding to I1125, M1169 and I1220 in HRV1A. When there is no cofactor or a drug in the pocket, the entrance to the pocket is open. However, the entrance is closed when the pocket is occupied by a cofactor or a drug. There are relatively small conformational changes when the agents displace the natural cofactor in HRV1A. In contrast, there are much larger conformational changes on binding a drug in HRV14. These differences cause an inhibition of viral attachment in HRV14 but not in HRV1A. Binding of the drugs results in three additional interprotomer hydrogen bonds in HRV14 and one in HRV1A. These hydrogen bonds and a potential loss of flexibility upon efficient packing of the pocket may contribute to the inhibition of uncoating in both serotypes.
+The line below this paragraph, {{ABSTRACT_PUBMED_8383771}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8383771 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8383771}}
 ==About this Structure==
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 [[Category: Icosahedral virus]]
 [[Category: Rhinovirus coat protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:47:38 2008''
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