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PDBsum entry 3hfm
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Complex(antibody-antigen)
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PDB id
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3hfm
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Contents |
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214 a.a.
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215 a.a.
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129 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of an antibody-Antigen complex: crystal structure of the hyhel-10 FAB-Lysozyme complex.
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Authors
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E.A.Padlan,
E.W.Silverton,
S.Sheriff,
G.H.Cohen,
S.J.Smith-Gill,
D.R.Davies.
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Ref.
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Proc Natl Acad Sci U S A, 1989,
86,
5938-5942.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen
egg white lysozyme has been determined to a nominal resolution of 3.0 A. The
antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of
residues from four different regions of the linear sequence. It consists of the
exposed residues of an alpha-helix together with surrounding amino acids. The
epitope crosses the active-site cleft and includes a tryptophan located within
this cleft. The combining site of the antibody is mostly flat with a
protuberance made up of two tyrosines that penetrate the cleft. All six
complementarity-determining regions of the Fab contribute at least one residue
to the binding; one residue from the framework is also in contact with the
lysozyme. The contacting residues on the antibody contain a disproportionate
number of aromatic side chains. The antibody-antigen contact mainly involves
hydrogen bonds and van der Waals interactions; there is one ion-pair interaction
but it is weak.
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Secondary reference #1
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Title
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A three-Dimensional model of an anti-Lysozyme antibody.
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Authors
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S.J.Smith-Gill,
C.Mainhart,
T.B.Lavoie,
R.J.Feldmann,
W.Drohan,
B.R.Brooks.
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Ref.
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J Mol Biol, 1987,
194,
713-724.
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PubMed id
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Secondary reference #2
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Title
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Crystalline monoclonal antibody fabs complexed to hen egg white lysozyme.
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Authors
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E.W.Silverton,
E.A.Padlan,
D.R.Davies,
S.Smith-Gill,
M.Potter.
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Ref.
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J Mol Biol, 1984,
180,
761-765.
[DOI no: ]
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PubMed id
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Figure 1.
ENID W. SILVERTON
EDUARDO A. PADLAN
DAVID R. DAVIES
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The above figure is
reproduced from the cited reference
with permission from Elsevier
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