(Q27648944)

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Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations

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Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations (English)

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crystal structure

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molecular dynamics simulation

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based on heuristic

inferred from abstract

structural biology

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based on heuristic

inferred from abstract

3C-like proteinase [SARS-Cov]

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based on heuristic

inferred from title

8

object named as

Xu Shen

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author name string

Shuai Chen

1

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Tiancen Hu

2

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Jian Zhang

3

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Jing Chen

4

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Kaixian Chen

5

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Jianping Ding

6

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Hualiang Jiang

7

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language of work or name

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publication date

4 January 2008

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Journal of Biological Chemistry

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283

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1

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554-64

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A previously undescribed coronavirus associated with respiratory disease in humans

1 reference

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Coronavirus as a possible cause of severe acute respiratory syndrome

1 reference

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Mechanisms and enzymes involved in SARS coronavirus genome expression

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Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs

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The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor

1 reference

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Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining the extra domain as a new target for design of highly specific protease inhibitors

1 reference

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Quaternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease

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Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase

1 reference

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Mechanism of the maturation process of SARS-CoV 3CL protease

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Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705240200

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Enzymatic activity of the SARS coronavirus main proteinase dimer.

1 reference

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pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses

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The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain

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Long-range cooperative interactions modulate dimerization in SARS 3CLpro.

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The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis

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Crystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide.

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Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations

1 reference

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Molecular cloning, expression, purification, and mass spectrometric characterization of 3C-like protease of SARS coronavirus

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Enzymatic activity characterization of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer technique

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Solvent content of protein crystals

1 reference

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MOLREP: an Automated Program for Molecular Replacement

1 reference

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The CCP4 suite: programs for protein crystallography

1 reference

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

1 reference

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Coot: model-building tools for molecular graphics

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Improved methods for building protein models in electron density maps and the location of errors in these models

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PROCHECK: a program to check the stereochemical quality of protein structures

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A solution for the best rotation to relate two sets of vectors

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Prediction of proteinase cleavage sites in polyproteins of coronaviruses and its applications in analyzing SARS-CoV genomes.

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Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes

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The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705240200

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Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer

1 reference

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Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction

1 reference

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Insight into the activity of SARS main protease: Molecular dynamics study of dimeric and monomeric form of enzyme.

1 reference

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3C-like proteinase from SARS coronavirus catalyzes substrate hydrolysis by a general base mechanism

1 reference

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The substrate specificity of SARS coronavirus 3C-like proteinase

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21 January 2018

Identifiers

10.1074/JBC.M705240200

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