1om3
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FAB 2G12 unliganded
OverviewOverview
Human antibody 2G12 neutralizes a broad range of human immunodeficiency, virus type 1 (HIV-1) isolates by binding an unusually dense cluster of, carbohydrate moieties on the "silent" face of the gp120 envelope, glycoprotein. Crystal structures of Fab 2G12 and its complexes with the, disaccharide Manalpha1-2Man and with the oligosaccharide Man9GlcNAc2, revealed that two Fabs assemble into an interlocked VH domain-swapped, dimer. Further biochemical, biophysical, and mutagenesis data strongly, support a Fab-dimerized antibody as the prevalent form that recognizes, gp120. The extraordinary configuration of this antibody provides an, extended surface, with newly described binding sites, for multivalent, interaction with a conserved cluster of oligomannose type sugars on the, surface of gp120. The unique interdigitation of Fab domains within an, antibody uncovers a previously unappreciated mechanism for high-affinity, recognition of carbohydrate or other repeating epitopes on cell or, microbial surfaces.
About this StructureAbout this Structure
1OM3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Antibody domain exchange is an immunological solution to carbohydrate cluster recognition., Calarese DA, Scanlan CN, Zwick MB, Deechongkit S, Mimura Y, Kunert R, Zhu P, Wormald MR, Stanfield RL, Roux KH, Kelly JW, Rudd PM, Dwek RA, Katinger H, Burton DR, Wilson IA, Science. 2003 Jun 27;300(5628):2065-71. PMID:12829775
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