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PDBsum entry 2iff
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Immunoglobulin/hydrolase(o-glycosyl)
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PDB id
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2iff
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Contents |
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212 a.a.
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214 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-Lysozyme complex unexpected effect of conservative mutation.
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Authors
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S.Chacko,
E.Silverton,
L.Kam-Morgan,
S.Smith-Gill,
G.Cohen,
D.Davies.
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Ref.
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J Mol Biol, 1995,
245,
261-274.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
94%.
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Abstract
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The structure of the complex between the Fab HyHEL-5 and chicken lysozyme
revealed a large interface region containing 23 lysozyme and 28 Fab residues.
Arg68 of the lysozyme is centrally placed in this interface and theoretical
studies together with binding assays of this Fab to different avian lysozymes
have previously shown that this arginine residue is an important contributor to
the binding. The Arg68-->Lys mutant binds 10(3) times less well to the
HyHEL-5 Fab. We have examined the refined crystal structure of the complex of
this mutant lysozyme with the Fab. No global changes occur, but there is an
introduction of a new water molecule into the interface that mediates the
hydrogen bonding interactions between the lysine and residues on the Fab. These
data are compared with the effects of similar changes on the inhibition of
serine proteases such as trypsin where the energetic effects of this
substitution are small.
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Figure 8.
Figure 8. Hydrogen bonding interactions around the 68(Y) pocket in the native and mutant structures.
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Figure 9.
Figure 9. Hydrogen bonding in the active site of the native and mutant BPTI--trypsin complexes.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1995,
245,
261-274)
copyright 1995.
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Secondary reference #1
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Title
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Three-Dimensional structure of an antibody-Antigen complex.
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Authors
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S.Sheriff,
E.W.Silverton,
E.A.Padlan,
G.H.Cohen,
S.J.Smith-Gill,
B.C.Finzel,
D.R.Davies.
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Ref.
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Proc Natl Acad Sci U S A, 1987,
84,
8075-8079.
[DOI no: ]
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PubMed id
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