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PDBsum entry 1fh5
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Immune system
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PDB id
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1fh5
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Contents |
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* Residue conservation analysis
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DOI no:
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J Biol Chem
276:3287-3294
(2001)
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PubMed id:
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The crystal structure of the fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone bip.
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J.G.Augustine,
A.de La Calle,
G.Knarr,
J.Buchner,
C.A.Frederick.
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ABSTRACT
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The Fab fragment of the murine monoclonal antibody, MAK33, directed against
human creatine kinase of the muscle-type, was crystallized and the
three-dimensional structure was determined to 2.9 A. The antigen-binding surface
of MAK33 shows a convex overall shape typical for immunoglobulins binding large
antigens. The structure allows us to analyze the environment of
cis-prolyl-peptide bonds whose isomerization is of key importance in the folding
process. These residues seem to be involved with not only domain stability but
also seem to play a role in the association of heavy and light chains,
reinforcing the importance of beta-strand recognition in antibody assembly. The
structure also allows the localization of segments of primary sequence
postulated to represent binding sites for the ER-specific chaperone BiP within
the context of the entire Fab fragment. These sequences are found primarily in
beta-strands that are necessary for interactions between the individual domains.
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Selected figure(s)
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Figure 3.
Fig. 3. Stereo models of cis-proline environments. Oxygen
atoms are red, carbon atoms are gray, and nitrogen atoms are
blue. Subsets of hydrogen bond distances are shown by dotted
lines. A, cis-ProL9; B, cis-ProH191; C, cis-ProL142; D,
cis-ProH149 and cis ProH151.
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Figure 4.
Fig. 4. Location of BiP-binding sites within MAK33 Fab.
Potential in vivo BiP-binding sites of the light and heavy
chains identified by the ability of the corresponding
heptapeptide to stimulate BiP-ATPase activity are highlighted on
the alpha carbon backbone trace of the Fab.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
3287-3294)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.J.Feige,
S.Groscurth,
M.Marcinowski,
Y.Shimizu,
H.Kessler,
L.M.Hendershot,
and
J.Buchner
(2009).
An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.
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Mol Cell,
34,
569-579.
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M.J.Feige,
S.Groscurth,
M.Marcinowski,
Z.T.Yew,
V.Truffault,
E.Paci,
H.Kessler,
and
J.Buchner
(2008).
The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.
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Proc Natl Acad Sci U S A,
105,
13373-13378.
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S.Frey,
M.Haslbeck,
O.Hainzl,
and
J.Buchner
(2008).
Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system.
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Biol Chem,
389,
37-45.
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S.C.Song,
M.Czerwinski,
B.S.Wojczyk,
and
S.L.Spitalnik
(2004).
Alteration of amino acid residues at the L-chain N-terminus and in complementarity-determining region 3 increases affinity of a recombinant F(ab) for the human N blood group antigen.
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Transfusion,
44,
173-186.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
