The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site (Q27733705)

2

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J A Wickersham

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Z Hostomsky

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N Habuka

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E W Moomaw

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T Adachi

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Z Hostomska

Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases

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language of work or name

English

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publication date

18 October 1996

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published in

Cell

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volume

87

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page(s)

331-42

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issue

2

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cites work

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Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase

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Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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Amino-aromatic interactions in proteins

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Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion

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Accurate bond and angle parameters for X-ray protein structure refinement

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Refined structure of alpha-lytic protease at 1.7 A resolution. Analysis of hydrogen bonding and solvent structure

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Identification of the protease domain in NS3 of hepatitis C virus

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The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution

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Molecular cloning of the human hepatitis C virus genome from Japanese patients with non-A, non-B hepatitis

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Aromatic rings act as hydrogen bond acceptors

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

3859327

3859327

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference