Cross‐strand disulphides in cell entry proteins: poised to act
- 19 December 2003
- Vol. 26 (1), 73-79
- https://doi.org/10.1002/bies.10413
Abstract
Cross‐strand disulphides (CSDs) are unusual bonds that link adjacent strands in the same β‐sheet. Their peculiarity relates to the high potential energy stored in these bonds, both as torsional energy in the highly strained disulphide linkage and as deformation energy stored in the sheet itself. CSDs are relatively rare in protein structures but are conspicuous by their presence in proteins that are involved in cell entry. The finding that entry of botulinum neurotoxin and HIV into mammalian cells involves cleavage of CSDs suggests that the activity of other cell entry proteins may likewise involve cleavage of these bonds. We examine emerging evidence of the involvement of these unusual disulphides in cell entry events. BioEssays 26:73–79, 2004.Keywords
This publication has 51 references indexed in Scilit:
- The Catalytic Activity of Protein Disulfide Isomerase Is Involved in Human Immunodeficiency Virus Envelope–Mediated Membrane Fusion after CD4 Cell BindingThe Journal of Infectious Diseases, 2001
- Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1999
- Sequence homology and structural analysis of the clostridial neurotoxinsJournal of Molecular Biology, 1999
- Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Å: evidence for conformational labilityJournal of Molecular Biology, 1999
- Crystal Structure of the Pertussis Toxin–ATP Complex: A Molecular SensorJournal of Molecular Biology, 1996
- The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolutionNature, 1995
- Structure of influenza haemagglutinin at the pH of membrane fusionNature, 1994
- Crystal Structure of Domains 3 and 4 of Rat CD4: Relation to the NH 2 -Terminal DomainsScience, 1993
- Elimination of the disulphide bridge in fragment B of diphtheria toxin: effect on membrane insertion, channel formation, and ATP bindingMolecular Microbiology, 1991
- Stimulation of the thiol-dependent ADP-ribosyltransferase and NAD glycohydrolase activities of Bordetella pertussis toxin by adenine nucleotides, phospholipids, and detergentsBiochemistry, 1986