Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active-site sequence of thiol-disulfide exchange enzymes.

Previous studies have indicated that the surface (SU) and transmembrane (TM) subunits of the envelope protein (Env) of murine leukemia viruses (MuLVs) are joined by a labile disulfide bond that can be stabilized by treatment of virions with thiol-specific reagents. In the present study this observat...

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Sparad:
Bibliografiska uppgifter
Huvudupphovsmän: Pinter, A, Kopelman, R, Li, Z, Kayman, S C, Sanders, D A
Materialtyp: Artigo
Språk:Inglês
Publicerad: 1997
Ämnen:
Research Article
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC192174/
https://ncbi.nlm.nih.gov/pubmed/9311907
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