Publication Date:
2006-07-15
Description:
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 alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heldwein, Ekaterina E -- Lou, Huan -- Bender, Florent C -- Cohen, Gary H -- Eisenberg, Roselyn J -- Harrison, Stephen C -- AI049980/AI/NIAID NIH HHS/ -- AI056045/AI/NIAID NIH HHS/ -- AI065886/AI/NIAID NIH HHS/ -- NS36731/NS/NINDS NIH HHS/ -- R21 AI065886/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):217-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA. heldwein@crystal.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840698" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Crystallization
;
Crystallography, X-Ray
;
Epitopes
;
Evolution, Molecular
;
Herpesvirus 1, Human/*chemistry
;
Hydrogen-Ion Concentration
;
Hydrophobic and Hydrophilic Interactions
;
Membrane Glycoproteins/chemistry/physiology
;
Models, Molecular
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protein Subunits/chemistry
;
Vesicular stomatitis Indiana virus/chemistry
;
Viral Envelope Proteins/*chemistry/immunology/physiology
;
Viral Fusion Proteins/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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