title: Sweet entanglements--protein:glycan interactions in two HIV-inactivating lectin families.
abstract: Structures and sugar binding by members of two lectin families, Cyanovirin-N homolog (CVNH) and Oscillatoria Agardhii agglutinin homolog (OAAH), were determined to elucidate the basis for recognition of high-mannose glycans on the HIV envelope glycoprotein gp120. We solved NMR solution and/or crystal structures for several lectins and delineated their carbohydrate specificity by array screening and direct NMR titrations. Both families recognize different epitopes on high-mannose glycans, namely, Manα(1-2)Man units at the end of the D1 and D3 arms and α3,α6-mannopentaose at the central branch point of Man-8 or Man-9 for CVNH and OAAH lectins, respectively.
authors.affiliation: Department of Structural Biology, School of Medicine, University of Pittsburgh, Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA. mik44@pitt.edu
authors.forename: Leonardus M I
authors.initials: LM
authors.lastname: Koharudin
authors.forename: Angela M
authors.initials: AM
authors.lastname: Gronenborn
mesh_terms: D000595:Amino Acid Sequence; D015497:HIV-1; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: D037102:Lectins; D011134:Polysaccharides; D011506:Proteins