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. Author manuscript; available in PMC: 2017 Jun 21.
Published in final edited form as: Biochemistry. 2016 Apr 4;55(15):2197–2213. doi: 10.1021/acs.biochem.5b01354

Figure 9.

Figure 9

Model of conformational and dynamic changes in the unliganded gp120 monomer upon deletion of V1/V2 and V3 loops. The unliganded wild-type full-length gp120 (FL) (left) had the highest dynamics in three layers of the inner domain with unfolded bridging sheets and masked immature coreceptor-binding site.96 Upon deletion of the V1/V2 and V3 loops, the three layers of the inner domain became less dynamic and more ordered. Coree without all V1/V2 and V3 loops showed more stability toward the CD4-bound state with an ordered inner domain and well-folded bridging sheets. The CD4 engagement (right) induced a fixed, stable conformation with formation of the bridging sheets and movement of V1/V2 loops to expose a mature coreceptor-binding site on the bridging sheet and V3 loop.