2hrv: Difference between revisions

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[[Image:2hrv.~~jpg~~|left|200px]]

[[Image:2hrv.png|left|200px]]

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~~'''~~2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2~~'''~~

===2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2===

~~==Overview==~~

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The ~~crystal structure of~~ the ~~2A proteinase from human rhinovirus serotype 2 (HRV2-2A(pro)) has been solved~~ to ~~1.95 A resolution. The structure has an unusual, although chymotrypsin-related, fold comprising a unique four-stranded beta sheet as~~ the ~~N-terminal domain and a six-stranded beta barrel~~ as ~~the C-terminal domain~~. ~~A tightly bound zinc ion, essential for the stability of HRV2-2A(pro~~), is ~~tetrahedrally coordinated by three cysteine sulfurs and one histidine nitrogen~~. ~~The active site consists of a catalytic triad formed by His18, Asp35 and Cys106. Asp35 is additionally involved in an extensive hydrogen~~-~~bonding network. Modelling studies reveal a substrate~~-~~induced fit that explains the specificity of the subsites S4, S2, S1 and S1'. The structure of HRV2-2A(pro) suggests the mechanism of the cis cleavage and its release from the polyprotein.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10523291}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10523291 is the PubMed ID number.

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==About this Structure==

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[[Category: Petersen, J F.W.]]

[[Category: Skern, T.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4~~ 06:~~38:20~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:06:24 2008''

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-[[Image:2hrv.jpg|left|200px]]
+{{Seed}}
+[[Image:2hrv.png|left|200px]]
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 {{STRUCTURE_2hrv|  PDB=2hrv  |  SCENE=  }}
-'''2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2'''
+===2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2===
-==Overview==
+<!--
-The crystal structure of the 2A proteinase from human rhinovirus serotype 2 (HRV2-2A(pro)) has been solved to 1.95 A resolution. The structure has an unusual, although chymotrypsin-related, fold comprising a unique four-stranded beta sheet as the N-terminal domain and a six-stranded beta barrel as the C-terminal domain. A tightly bound zinc ion, essential for the stability of HRV2-2A(pro), is tetrahedrally coordinated by three cysteine sulfurs and one histidine nitrogen. The active site consists of a catalytic triad formed by His18, Asp35 and Cys106. Asp35 is additionally involved in an extensive hydrogen-bonding network. Modelling studies reveal a substrate-induced fit that explains the specificity of the subsites S4, S2, S1 and S1'. The structure of HRV2-2A(pro) suggests the mechanism of the cis cleavage and its release from the polyprotein.
+The line below this paragraph, {{ABSTRACT_PUBMED_10523291}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10523291 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10523291}}
 ==About this Structure==
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 [[Category: Petersen, J F.W.]]
 [[Category: Skern, T.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:38:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:06:24 2008''