VRC01 gp120 complex: Difference between revisions

<u>Similarities to CD4 in complex with gp120</u>. Analysis of VRC01 in complex with gp120 shows that this complex covers 98% of the CD4 binding site.  However, VRC01’s binding site extends outside that of CD4, making it vulnerable to resistance of VRC01 neutralization by antigenic variation. [[Image: Target Site.jpg | thumb | alt=text | Picture 1]] Both the heavy chain and light chain of VRC01 contribute to the contact surfaces of the VRC01 gp120 complex.  The focus of the binding is on the heavy chain second complementary-determining region.  Over 50% of the surface contact involves the heavy chain second complementary-determining region; this is similar to CD4’s interaction with gp120.  Two dominant residues, Phe43 and Arg59, are involved in CD4’s binding to gp120.  Of these two residues, only the arginine interaction is mimicked by VRC01. This dominant interaction is between Asp368 of gp120 and Arg59 of the CD4 receptor and between Asp368 of gp120 and Arg71 of VRC01<ref name="zhou">PMID: 20616231</ref>.