Figure 7. . Structure of the baculovirus F (fusion) protein (Ld130) from LdMNPV and AcMNPV GP64.

Figure 7.

Structure of the baculovirus F (fusion) protein (Ld130) from LdMNPV and AcMNPV GP64. A) Ld130 F protein. Shown is a predicted signal peptide (SP), fusion peptide (FP) and transmembrane domain (TM) including the amino acid coordinates. The cleavage site is indicated by the arrow. A predicted coiled coil domain is also indicated. The disulfide bond is predicted from (215). B) GP64. This figure is derived from Kadlec (60). Shown are 7 disulfide bonds, all of which are intramolecular except for the one from aa 24 which is connected to aa 372 in an adjacent molecule. This and the coiled-coil (299-341) region are involved in trimer formation. All the disulfide bonds are conserved except 178-184 which is not present in thogotovirus GP64. The receptor binding/fusion peptide region is shown at the base of the diagram. From Kadlec et al (60).

Copyright 2008 by Nature Publishing Group.

Reproduced with permission of Nature Publishing Group via Copyright Clearance Center.

From: Chapter 2, Structural proteins of baculovirus occlusion bodies and virions

Cover of Baculovirus Molecular Biology
Baculovirus Molecular Biology [Internet]. 3rd edition.
Rohrmann GF.
Bethesda (MD): National Center for Biotechnology Information (US); 2013.
Copyright © 2013, George Rohrmann.

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