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PDBsum entry 1igc
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Complex (antibody/binding protein)
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PDB id
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1igc
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Contents |
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213 a.a.
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222 a.a.
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58 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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The third igg-Binding domain from streptococcal protein g. An analysis by X-Ray crystallography of the structure alone and in a complex with FAB.
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Authors
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J.P.Derrick,
D.B.Wigley.
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Ref.
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J Mol Biol, 1994,
243,
906-918.
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PubMed id
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Abstract
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Protein G is a cell surface-associated protein from Streptococcus that binds to
IgG with high affinity. We have determined the X-ray crystal structures of the
third IgG-binding domain (domain III) alone to a resolution of 1.1 A (final
R-factor of 19.3%), and in complex with an Fab fragment to 2.6 A (final R-factor
of 16.8%). The structure of domain III is similar to the lower-resolution
crystal structures of protein G domains determined previously by other
investigators, but shows some minor differences when compared with the
equivalent NMR structures. Domain III binds to the immunoglobulin by formation
of an antiparallel interaction between the second beta-strand in domain III and
the last beta-strand in the CH 1 domain. There is also a minor site of
interaction between the C-terminal end of the alpha-helix in protein G and the
first beta-strand in the CH 1 domain. Previous studies by NMR on the
interactions between protein G and IgG have concluded that different portions of
the protein G domain are involved in binding to the Fab and Fc portions. The
results presented here support these findings and permit a detailed analysis of
the recognition of Fab by protein G; formation of the complex buries a large
water-accessible area, of a magnitude comparable with that found in
antibody/antigen interactions. The majority of hydrogen bonds between the two
proteins involve main-chain atoms from the CH 1 domain. The CH 1 domain residues
that are in contact with protein G are shown to be highly conserved in
alignments of mouse and human gamma chain amino acid sequences. We conclude that
the binding site for protein G on Fab is relatively invariant across different
species and gamma chain subclasses, providing an explanation for the widespread
recognition of Fab fragments from mouse and human antibodies by protein G. The
solution of the crystal structures of domain III alone and bound to Fab has
demonstrated that there is no major structural change apparent in either protein
on formation of the complex.
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Secondary reference #1
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Title
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Two crystal structures of the b1 immunoglobulin-Binding domain of streptococcal protein g and comparison with nmr.
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Authors
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T.Gallagher,
P.Alexander,
P.Bryan,
G.L.Gilliland.
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Ref.
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Biochemistry, 1994,
33,
4721-4729.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Crystal structure of a streptococcal protein g domain bound to an FAB fragment.
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Authors
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J.P.Derrick,
D.B.Wigley.
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Ref.
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Nature, 1992,
359,
752-754.
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PubMed id
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Secondary reference #3
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Title
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Crystallization and preliminary X-Ray analysis of the complex between a mouse FAB fragment and a single igg-Binding domain from streptococcal protein g.
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Authors
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J.P.Derrick,
G.J.Davies,
Z.Dauter,
K.S.Wilson,
D.B.Wigley.
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Ref.
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J Mol Biol, 1992,
227,
1253-1254.
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PubMed id
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Secondary reference #4
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Title
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Determination of the solution structures of domains ii and III of protein g from streptococcus by 1h nuclear magnetic resonance.
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Authors
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L.Y.Lian,
J.P.Derrick,
M.J.Sutcliffe,
J.C.Yang,
G.C.Roberts.
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Ref.
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J Mol Biol, 1992,
228,
1219-1234.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. ``Sticky foot'' mutagenesis cloning of domain
II and domain HI. An asterisk denotes restriction sites
inserted during the utagenesis procedure.
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Figure 12.
Figure 12. Stereo view of the 2 cnformations in the region Gly43-Asp45 adopted by domain III showing the
backbone aoms (N, C'' and C'). The minor conformation is shown in bold and the major conformation is shown with a
broken line. The structures have been superposed on the average structure using backbone atoms (N, c'' and C':I in the
secondary structural elements.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #5
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Title
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1.67-A X-Ray structure of the b2 immunoglobulin-Binding domain of streptococcal protein g and comparison to the nmr structure of the b1 domain.
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Authors
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A.Achari,
S.P.Hale,
A.J.Howard,
G.M.Clore,
A.M.Gronenborn,
K.D.Hardman,
M.Whitlow.
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Ref.
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Biochemistry, 1992,
31,
10449-10457.
[DOI no: ]
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PubMed id
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Secondary reference #6
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Title
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A novel, Highly stable fold of the immunoglobulin binding domain of streptococcal protein g.
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Authors
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A.M.Gronenborn,
D.R.Filpula,
N.Z.Essig,
A.Achari,
M.Whitlow,
P.T.Wingfield,
G.M.Clore.
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Ref.
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Science, 1991,
253,
657-661.
[DOI no: ]
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PubMed id
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