Predicted 3D Model of the Rabies Virus Glycoprotein Trimer

Figure 3

Domains of glycoprotein. The top lateral domain (DI) contains about 90 residues in two segments (1 to 17 and 312 to 383). Trimerization domain (DII) is made of three segments (18 to 35, 259 to 311, and 384 to 409), PH domain (DIII) is inserted within domain II. It is made of two segments (36 to 50 and 181 to 258) and has the fold of a pH domain. Fusion (DIV) (51 to 180) is inserted in a loop of the pH domain and is made of an extended sheet structure at the tip of which two loops are located that constitute the membrane-interacting motif of the G ectodomain. (a) Glycoprotein monomeric divided into 4 domains: DI (red) is lateral domain, DII (blue) is trimerization domain, DIII (orange) is domain of pH, and DIV (yellow) is fusion domain. (b) Surface representation of glycoprotein monomeric colored by domains. (c) Top view of the trimer, colored by domain, shows the formation of 6 alpha helices (blue) which contribute to the stability of the structure. (d) Top view of the trimer surface representation. (e) Glycoprotein trimer (divided into different domains) does not show a significant change in the organization of the domains. (f) Surface representation of the glycoprotein trimer, showing the cavity inside the molecule.

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