About: Structural comparison strengthens the higher-order classification of proteases related to chymotrypsin

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

About: Structural comparison strengthens the higher-order classification of proteases related to chymotrypsin 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	Structural comparison strengthens the higher-order classification of proteases related to chymotrypsin
Creator	Mö, Heli Poranen Id, Minna Ravantti,
Source	Medline; PMC
abstract	Specific cleavage of proteins by proteases is essential for several cellular, physiological, and viral processes. Chymotrypsin-related proteases that form the PA clan in the MEROPS classification of proteases is one of the largest and most diverse group of proteases. The PA clan comprises serine proteases from bacteria, eukaryotes, archaea, and viruses and chymotrypsin-related cysteine proteases from positive-strand RNA viruses. Despite low amino acid sequence identity, all PA clan proteases share a conserved double β-barrel structure. Using an automated structure-based hierarchical clustering method, we identified a common structural core of 72 amino acid residues for 143 PA clan proteases that represent 12 protein families and 11 subfamilies. The identified core is located around the catalytic site between the two β-barrels and resembles the structures of the smallest PA clan proteases. We constructed a structure-based distance tree derived from the properties of the identified common core. Our structure-based analyses support the current classification of these proteases at the subfamily level and largely at the family level. Structural alignment and structure-based distance trees could thus be used for directing objective classification of PA clan proteases and to strengthen their higher order classification. Our results also indicate that the PA clan proteases of positive-strand RNA viruses are related to cellular heat-shock proteases, which suggests that the exchange of protease genes between viruses and cells might have occurred more than once.
has issue date	2019-05-17(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0216659
bibo:pmid	31100077
has license	cc-by
sha1sum (hex)	7a8b68779090a6be24461fb2b19c974232899889
schema:url	https://doi.org/10.1371/journal.pone.0216659
resource representing a document's title	Structural comparison strengthens the higher-order classification of proteases related to chymotrypsin
has PubMed Central identifier	PMC6524800
has PubMed identifier	31100077
schema:publication	PLoS One
resource representing a document's body	covid:7a8b68779090a6be24461fb2b19c974232899889#body_text
is schema:about of	named entity 'proteases' named entity 'proteases' named entity 'Structural' named entity 'represent' named entity 'STRUCTURAL' named entity 'MEROPS' named entity 'DERIVED' named entity 'SUBFAMILY' named entity 'OBJECTIVE' named entity 'POSITIVE' named entity 'MORE THAN ONCE' named entity 'LARGELY' named entity 'PROPERTIES' named entity 'CELLULAR' named entity 'HAVE' named entity 'AUTOMATED' named entity 'GENES' named entity 'SEQUENCE IDENTITY' named entity 'ARCHAEA' named entity 'DISTANCE' named entity '143' named entity 'CHYMOTRYPSIN' named entity 'TREE' named entity 'SMALLEST' named entity 'OUR' named entity 'CLEAVAGE' named entity 'TREES' named entity 'GROUP' named entity 'EXCHANGE' named entity 'RELATED' named entity 'CLAN' named entity 'RESULTS' named entity 'STRUCTURES' named entity 'VIRUSES' named entity 'BASED' named entity 'PROTEINS' named entity 'CATALYTIC SITE' named entity 'BACTERIA' named entity 'DOUBLE' named entity 'LOW' named entity 'PROTEIN FAMILIES' named entity 'COMPARISON' named entity 'CONSTRUCTED' named entity 'FAMILY' named entity 'HTTPS' named entity 'ORDER' named entity 'COMMON' named entity 'ONE OF' named entity 'CORE' named entity 'PHYSIOLOGICAL' named entity 'USING' named entity 'PROTEASES' named entity 'ORDER' named entity 'HIGHER' named entity 'STRUCTURE' named entity 'HIGHER' named entity 'CYSTEINE PROTEASES' covid:arg/7a8b68779090a6be24461fb2b19c974232899889 named entity 'PROTEASES' named entity 'DIVERSE' named entity 'LEVEL' named entity 'RELATED' named entity 'FORM' named entity 'CLASSIFICATION' named entity 'COMPARISON' named entity 'CHYMOTRYPSIN' named entity 'VIRAL' named entity 'METHOD' named entity 'STRUCTURAL ALIGNMENT' named entity 'SHARE' named entity 'USED' named entity 'CONSERVED' named entity 'STRAND' named entity 'IDENTIFIED' named entity 'THESE' named entity 'PROTEASE' named entity 'AMINO ACID' named entity 'AMINO ACID SEQUENCE' named entity 'SUPPORT'

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