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Article

Mutations in herpes simplex virus gD protein affect receptor binding by different molecular mechanisms.

Journal of molecular modeling - 1 Apr 2014

Stump Joachim D, Sticht Heinrich

Abstract excerpt

Glycoprotein D (gD) is an essential protein of herpes simplex virus-1 (HSV-1) that targets the structurally unrelated receptors HVEM and nectin-1. Receptor binding of gD is accompanied by intramolecular structural rearrangements including the detachment of the C-terminus or formation of an N-terminal hairpin structure. We have investigated several gD mutations that were reported to affect receptor binding...

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Identifiers

PMID: 24647818
DOI: 10.1007/s00894-014-2192-x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Mutations in herpes simplex virus gD protein affect receptor binding by different molecular mechanisms.PMID 24647818Read ↗

Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface.Semantic proximity Read ↗

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Nectin2alpha (PRR2alpha or HveB) and nectin2delta are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D.Semantic proximity Read ↗

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