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PDBsum entry 3ijh
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Immune system
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PDB id
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3ijh
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References listed in PDB file
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Key reference
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Title
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The role of cdr h3 in antibody recognition of a synthetic analog of a lipopolysaccharide antigen.
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Authors
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C.L.Brooks,
R.J.Blackler,
G.Sixta,
P.Kosma,
S.Müller-Loennies,
L.Brade,
T.Hirama,
C.R.Mackenzie,
H.Brade,
S.V.Evans.
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Ref.
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Glycobiology, 2010,
20,
138-147.
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PubMed id
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Abstract
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In order to explore the structural basis for adaptability in near germline
monoclonal antibodies (mAb), we have examined the specificity of the promiscuous
mAb S67-27 to both naturally derived carbohydrate antigens and a variety of
synthetic nonnatural antigens based on the bacterial lipopolysaccharide
component 3-deoxy-alpha-D-manno-oct-2-ulosonic acid (Kdo). One such analog, a
7-O-methyl (7-O-Me) Kdo disaccharide, was found to bind to the antibody with at
least 30-fold higher affinity than any other antigen tested. The structure of
S67-27 in complex with this analog and three other naturally occurring Kdo
antigens revealed that the enhanced affinity of the mAb for the synthetic analog
was accomplished by the strategic positioning of CDR H3 away from a conserved
Kdo binding pocket that allowed the formation of new antibody-antigen contacts.
Furthermore, the comparison of this structure with the structures of related
mAbs revealed how the position and structure of CDR H3 influence the specificity
or promiscuity of near-germline carbohydrate-recognizing antibodies by altering
the architecture of the combining site.
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