Science (American Association for the Advancement of Science), 2006-07, Vol.313 (5784), p.217-220
2006
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Crystal Structure of Glycoprotein B from Herpes Simplex Virus 1
- Ist Teil von
- Science (American Association for the Advancement of Science), 2006-07, Vol.313 (5784), p.217-220
- Ort / Verlag
- Washington, DC: American Association for the Advancement of Science
- Erscheinungsjahr
- 2006
- Quelle
- American Association for the Advancement of Science
- Beschreibungen/Notizen
- Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An α-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended β hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.1126548Titel-ID: cdi_proquest_miscellaneous_68627620
- Format
- –
- Schlagworte
- Amino Acid Sequence, Biological and medical sciences, Crystal structure, Crystallization, Crystallography, X-Ray, Epitopes, Evolution, Molecular, Fundamental and applied biological sciences. Psychology, Glycoproteins, Herpes simplex virus 1, Herpes viruses, Herpesviridae, Herpesvirus 1, Human - chemistry, Human herpesvirus 1, Hydrogen-Ion Concentration, Hydrophobic and Hydrophilic Interactions, Membrane Glycoproteins - chemistry, Membrane Glycoproteins - physiology, Microbiology, Models, Molecular, Molecular Sequence Data, Molecules, Morphology, structure, chemical composition, physicochemical properties, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Protein subunits, Protein Subunits - chemistry, Proteins, Trimers, Vesicular stomatitis Indiana virus - chemistry, Viral Envelope Proteins - chemistry, Viral Envelope Proteins - immunology, Viral Envelope Proteins - physiology, Viral Fusion Proteins - chemistry, Virology, Viruses