2lqy

Structure and orientation of the gH625-644 membrane interacting region of herpes simplex virus type 1 in a membrane mimetic system.

spinqualitylabelsall models 2lqy Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lqy is a 1 chain structure with sequence from Human alphaherpesvirus 1. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GH_HHV11 The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis.[HAMAP-Rule:MF_04033] Publication Abstract from PubMed Glycoprotein H (gH) of the herpes simplex virus type 1 is involved in the complex mechanism of membrane fusion of the viral envelope with host cells. The virus requires four glycoproteins (gB, gD, gH, gL) to execute fusion and the role played by gH remains mysterious. Mutational studies have revealed several regions of gH ectodomain required for fusion and identified the segment from amino acid 625 to 644 as the most fusogenic region. Here, we studied the behavior in a membrane-mimicking DPC micellar environment of a peptide encompassing this region (gH625-644) and determined its NMR solution structure and its orientation within the micelles. Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System.,Galdiero S, Russo L, Falanga A, Cantisani M, Vitiello M, Fattorusso R, Malgieri G, Galdiero M, Isernia C Biochemistry. 2012 Apr 10;51(14):3121-8. Epub 2012 Mar 23. PMID:22397737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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