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

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure
Creator	Jiang, Hualiang Chen, Jing Shen, Xu Chen, Shuai Zhang, Yu Li, Lianwei Ding, Jianping Hu, Tiancen Wang, Kuifeng
Source	Elsevier; Medline; PMC
abstract	Abstract The 3C-like protease of SARS coronavirus (SARS-CoV 3CLpro) is vital for SARS-CoV replication and is a promising drug target. It has been extensively proved that only the dimeric enzyme is active. Here we discovered that two adjacent mutations (Ser139_Ala and Phe140_Ala) on the dimer interface resulted in completely different crystal structures of the enzyme, demonstrating the distinct roles of these two residues in maintaining the active conformation of SARS-CoV 3CLpro. S139A is a monomer that is structurally similar to the two reported monomers G11A and R298A. However, this mutant still retains a small fraction of dimer in solution, which might account for its remaining activity. F140A is a dimer with the most collapsed active pocket discovered so far, well-reflecting the stabilizing role of this residue. Moreover, a plausible dimerization mechanism was also deduced from structural analysis. Our work is expected to provide insight on the dimerization–function relationship of SARS-CoV 3CLpro.
has issue date	2009-06-05(xsd:dateTime)
bibo:doi	10.1016/j.virol.2009.03.034
bibo:pmid	19409595
has license	els-covid
sha1sum (hex)	cc0b62cf9592001ab3629db667ac8474e612aa1d
schema:url	https://doi.org/10.1016/j.virol.2009.03.034
resource representing a document's title	Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure
has PubMed Central identifier	PMC7103376
has PubMed identifier	19409595
schema:publication	Virology
resource representing a document's body	covid:cc0b62cf9592001ab3629db667ac8474e612aa1d#body_text
is schema:about of	named entity 'LIKE' named entity 'MUTATIONS' named entity 'INTERFACE' named entity 'residues' named entity 'pro' named entity 'pocket' named entity 'expected' named entity 'vital' named entity 'enzyme' named entity 'structural analysis' named entity 'DIMER' named entity 'DIFFERENT' named entity 'PROTEASE' named entity 'SOLUTION' named entity 'RELATIONSHIP' named entity 'RETAINS' named entity 'VITAL' named entity 'MUTATIONS' named entity 'IS A' named entity 'ADJACENT' named entity 'OUR' named entity 'ACCOUNT' named entity 'DISTINCT' covid:arg/cc0b62cf9592001ab3629db667ac8474e612aa1d named entity 'CONFORMATION' named entity 'ROLE' named entity 'DIFFERENT' named entity 'WORK' named entity 'CRYSTAL' named entity 'REFLECTING' named entity 'MAINTAINING' named entity 'INSIGHT' named entity 'SARS-COV' named entity 'PRO' named entity 'REMAINING' named entity 'TO PROVIDE' named entity 'ENZYME' named entity 'ACTIVITY' named entity 'CHANGES' named entity 'SARS CORONAVIRUS' named entity 'INTERFACE' named entity 'MONOMER' named entity 'ALA' named entity 'CRYSTAL STRUCTURE' named entity 'RESIDUE' named entity 'STRUCTURAL ANALYSIS' named entity 'COMPLETELY' named entity 'MONOMERS' named entity 'MUTANT' named entity 'STABILIZING' named entity 'ITS' named entity 'CAUSE' named entity 'SARS CORONAVIRUS' named entity 'HERE' named entity 'STRUCTURES' named entity 'REPLICATION' named entity 'ADJACENT' named entity 'FRACTION OF' named entity 'SMALL' named entity 'FAR' named entity 'COLLAPSED' named entity 'ROLES' named entity 'ACTIVE' named entity 'DRUG TARGET' named entity 'MECHANISM' named entity 'PROTEASE' named entity 'THESE' named entity 'DIMER' named entity 'EXPECTED' named entity 'LIKE' named entity 'SIMILAR' named entity 'DIMERIZATION' named entity 'FUNCTION'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software