Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure (Q27655351)

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English	Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure	scientific article

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scholarly article

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Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure (English)

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crystal structure

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1 reference

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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1 reference

based on heuristic

inferred from title

9

object named as

Xu Shen

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author name string

Tiancen Hu

1

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Yu Zhang

2

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Lianwei Li

3

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Kuifeng Wang

4

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Shuai Chen

5

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Jing Chen

6

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Jianping Ding

7

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Hualiang Jiang

8

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language of work or name

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publication date

5 June 2009

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388

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2

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324-34

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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain

1 reference

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

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Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro.

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The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity

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Deubiquitinating Activity of the SARS-CoV Papain-Like Protease

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

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

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Reversible unfolding of the severe acute respiratory syndrome coronavirus main protease in guanidinium chloride

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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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Only one protomer is active in the dimer of SARS 3C-like proteinase

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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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

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Residues on the dimer interface of SARS coronavirus 3C-like protease: dimer stability characterization and enzyme catalytic activity analysis

1 reference

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

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The CCP4 suite: programs for protein crystallography

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Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus

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

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A previously undescribed coronavirus associated with respiratory disease in humans

1 reference

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Enzymatic activity of the SARS coronavirus main proteinase dimer.

1 reference

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SARS CoV main proteinase: The monomer-dimer equilibrium dissociation constant

1 reference

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

1 reference

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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://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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A novel coronavirus associated with severe acute respiratory syndrome

1 reference

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Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Proteomic analysis of up-regulated proteins in human promonocyte cells expressing severe acute respiratory syndrome coronavirus 3C-like protease

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Severe acute respiratory syndrome coronavirus 3C-like protease-induced apoptosis

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Correlation between dissociation and catalysis of SARS-CoV main protease.

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Refinement of macromolecular structures by the maximum-likelihood method

1 reference

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Coronavirus as a possible cause of severe acute respiratory syndrome

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme

1 reference

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Mechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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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

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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SARS: systematic review of treatment effects

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease?

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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

1 reference

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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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

1 reference

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Mechanisms and enzymes involved in SARS coronavirus genome expression

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1 reference

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

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Crystal structure of HAb18G/CD147: implications for immunoglobulin superfamily homophilic adhesion

1 reference

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Without its N-finger, the main protease of severe acute respiratory syndrome coronavirus can form a novel dimer through its C-terminal domain.

1 reference

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Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase.

2 references

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https://api.crossref.org/works/10.1016%2FJ.VIROL.2009.03.034

7 January 2021

based on heuristic

inferred from DOI database lookup

Virus-encoded proteinases and proteolytic processing in the Nidovirales.

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103376

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

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7 January 2021

MOLREP: an Automated Program for Molecular Replacement

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https://api.crossref.org/works/10.1016%2FJ.VIROL.2009.03.034

7 January 2021

Identifiers

10.1016/J.VIROL.2009.03.034

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