About: Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4

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About: Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4 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
title	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
Creator	Jiang, Liwei Shi, Xuanling Wang, Dongli Wang, Xinquan Zhang, Linqi Zhang, Senyan Wang, Nianshuang Liu, Xi Cui, Ye Fu, Lili Arledge, Kelly Chen, Ying-Hua Guo, Dongxing Tong, Pei
topic	covid:18d7f4c8e204349b39a037c19874cff1b34d0f97#this
source	Medline; PMC
abstract	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4). Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction. We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4. Our results show that MERS-CoV RBD consists of a core and a receptor-binding subdomain. The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain. MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain. Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell. The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
has issue date	2013-07-09(xsd:dateTime)
bibo:doi	10.1038/cr.2013.92
bibo:pmid	23835475
has license	cc-by-nc-nd
sha1sum (hex)	18d7f4c8e204349b39a037c19874cff1b34d0f97
schema:url	https://doi.org/10.1038/cr.2013.92
resource representing a document's title	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
has PubMed Central identifier	PMC3731569
has PubMed identifier	23835475
schema:publication	Cell Res
resource representing a document's body	covid:18d7f4c8e204349b39a037c19874cff1b34d0f97#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/18d7f4c8e204349b39a037c19874cff1b34d0f97
is schema:about of	named entity 'BINDING' named entity 'MERS-COV' named entity 'DPP4' named entity 'ITS' named entity 'MUTAGENESIS' named entity 'TARGET CELL' named entity 'THERAPEUTICS' named entity 'STRUCTURAL' named entity 'OUR' named entity 'RECEPTORBINDING' named entity 'VIRAL' named entity 'DEVELOPMENT' named entity '28S' named entity 'ENTRY' named entity 'DEGREE' named entity 'VACCINES' named entity 'SARS-COV' named entity 'CRYSTAL STRUCTURE' named entity 'INTERFACE' named entity 'CELLULAR' named entity 'SEQUENCE COMPARISON' named entity 'ATOMIC' named entity 'REVEALED' named entity 'RBD' named entity 'key' named entity 'domain' named entity 'degree' named entity 'identified' named entity 'Our' named entity 'Mutagenesis' named entity 'consists' named entity 'structural similarity' named entity 'RBD' named entity 'receptor' named entity 'RECEPTOR' named entity 'BUT' named entity 'RBD' named entity 'HUMAN' named entity 'TARGETS' named entity 'SPIKE' named entity 'KEY' named entity 'INTRINSIC' named entity 'HYDROLASE' named entity 'HIGH' named entity 'REPORT' named entity 'MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS' named entity 'BINDING' named entity 'DOMAIN' named entity 'COMPLEX' named entity 'DETAILS' named entity 'EXTRACELLULAR DOMAIN' named entity 'MEDIATES' named entity 'CORE' named entity 'RELATED' named entity 'CRITICAL' named entity 'INTERACTION' named entity 'INFECTION' named entity 'BOUND' named entity 'RECEPTOR INTERACTION' named entity 'UNDERSTANDING' named entity 'SIMILARITY' named entity 'STUDIES' named entity 'SUBDOMAIN' named entity 'DIPEPTIDYL PEPTIDASE 4' named entity 'RECENTLY' named entity 'RBD'

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