2LQY
Structure and orientation of the gH625-644 membrane interacting region of herpes simplex virus type 1 in a membrane mimetic system.
Summary for 2LQY
| Entry DOI | 10.2210/pdb2lqy/pdb |
| NMR Information | BMRB: 18335 |
| Descriptor | Envelope glycoprotein H (1 entity in total) |
| Functional Keywords | viral protein |
| Biological source | Human herpesvirus 1 (HHV-1) |
| Total number of polymer chains | 1 |
| Total formula weight | 2302.64 |
| Authors | Isernia, C.,Galdiero, S.,Russo, L.,Falanga, A.,Cantisani, M.,Vitiello, M.,Fattorusso, R.,Malgieri, G.,Galdiero, M. (deposition date: 2012-03-19, release date: 2012-04-25, Last modification date: 2024-05-15) |
| Primary citation | Galdiero, S.,Russo, L.,Falanga, A.,Cantisani, M.,Vitiello, M.,Fattorusso, R.,Malgieri, G.,Galdiero, M.,Isernia, C. Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System. Biochemistry, 51:3121-3128, 2012 Cited by PubMed Abstract: 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. PubMed: 22397737DOI: 10.1021/bi201589m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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