About: Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics

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About: Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics
Creator	Graul, Małgorzata Karska, Natalia Kasprzykowski, Franciszek Rodziewicz-Motowidło, Sylwia Sikorska, Emilia Zhukov, Igor Lipińska, Andrea
Source	Elsevier; Medline; PMC
abstract	Abstract The transporter associated with antigen processing (TAP) directly participates in the immune response as a key component of the cytosolic peptide to major histocompatibility complex (MHC) class I protein loading machinery. This makes TAP an important target for viruses avoiding recognition by CD8+ T lymphocytes. Its activity can be suppressed by the UL49.5 protein produced by bovine herpesvirus 1, although the mechanism of this inhibition has not been understood so far. Therefore, the main goal of our study was to investigate the 3D structure of bovine herpesvirus 1 - encoded UL49.5 protein. The final structure of the inhibitor was established using circular dichroism (CD), 2D nuclear magnetic resonance (NMR), and molecular dynamics (MD) in membrane mimetic environments. In NMR studies, UL49.5 was represented by two fragments: the extracellular region (residues 1–35) and the transmembrane-intracellular fragment (residues 36–75), displaying various functions during viral invasion. After the empirical structure determination, a molecular docking procedure was used to predict the complex of UL49.5 with the TAP heterodimer. Our results revealed that UL49.5 adopted a highly flexible membrane-proximal helical structure in the extracellular part. In the transmembrane region, we observed two short α-helices. Furthermore, the cytoplasmic part had an unordered structure. Finally, we propose three different orientations of UL49.5 in the complex with TAP. Our studies provide, for the first time, the experimental structural information on UL49.5 and structure-based insight in its mechanism of action which might be helpful in designing new drugs against viral infections.
has issue date	2019-05-01(xsd:dateTime)
bibo:doi	10.1016/j.bbamem.2019.02.005
bibo:pmid	30772281
has license	els-covid
sha1sum (hex)	93bc6ce303e06f82acc73b792734a10caaeb1e6d
schema:url	https://doi.org/10.1016/j.bbamem.2019.02.005
resource representing a document's title	Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics
has PubMed Central identifier	PMC7089609
has PubMed identifier	30772281
schema:publication	Biochimica et Biophysica Acta (BBA) - Biomembranes
resource representing a document's body	covid:93bc6ce303e06f82acc73b792734a10caaeb1e6d#body_text
is schema:about of	named entity 'TRANSMEMBRANE PROTEIN' named entity 'key' named entity 'I PROTEIN' named entity 'ACTIVITY' named entity 'IMPORTANT' named entity 'MACHINERY' named entity 'MOLECULAR DYNAMICS' named entity 'BOVINE HERPESVIRUS 1' named entity 'PEPTIDE' named entity 'KEY' named entity 'BOVINE HERPESVIRUS 1' named entity 'IMMUNE RESPONSE' named entity 'STRUCTURE DETERMINATION' named entity 'PROTEIN ' named entity 'DIRECTLY' named entity 'INHIBITION' named entity 'SUPPRESSED' named entity 'VIRUSES' named entity 'COMPONENT' named entity 'CD8' named entity 'CYTOSOLIC' named entity 'MECHANISM' named entity 'LOADING' named entity 'T LYMPHOCYTES' named entity 'RECOGNITION' named entity 'ITS' named entity 'UL49.5' named entity 'CLASS I' named entity 'UNDERSTOOD' named entity 'MAJOR HISTOCOMPATIBILITY COMPLEX' named entity 'TAP' named entity 'TARGET' named entity 'UL49.5' named entity 'NMR SPECTROSCOPY' named entity 'TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING' named entity 'FAR' named entity 'PROTEIN ' covid:arg/93bc6ce303e06f82acc73b792734a10caaeb1e6d named entity 'bovine herpesvirus 1' named entity 'cytosolic' named entity 'peptide' named entity 'molecular dynamics' named entity 'transmembrane protein' named entity 'transmembrane' named entity 'amino acid residue' named entity 'ultraviolet' named entity 'inclusion bodies' named entity 'conformation' named entity 'arginine' named entity 'substrate' named entity 'trifluoroacetic acid' named entity 'substrate' named entity 'molecular docking' named entity 'fully exposed' named entity 'C-terminal' named entity 'peptide' named entity 'peptide' named entity 'A63' named entity 'protein' named entity 'BHV-1' named entity 'positively charged' named entity 'PyMOL' named entity 'peptide bond' named entity 'transmembrane domain' named entity 'peptide' named entity 'hydrophobic core' named entity 'interact' named entity 'N-terminal region' named entity 'Proline' named entity 'R74' named entity 'POPC' named entity 'peptide' named entity 'E70' named entity 'proteasome' named entity 'dimethylation'

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