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* Residue conservation analysis
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J Immunol
165:6422-6428
(2000)
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PubMed id:
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Three-dimensional structure of the Fab from a human IgM cold agglutinin.
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A.Cauerhff,
B.C.Braden,
J.G.Carvalho,
R.Aparicio,
I.Polikarpov,
J.Leoni,
F.A.Goldbaum.
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ABSTRACT
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Cold agglutinins (CAs) are IgM autoantibodies characterized by their ability to
agglutinate in vitro RBC at low temperatures. These autoantibodies cause
hemolytic anemia in patients with CA disease. Many diverse Ags are recognized by
CAs, most frequently those belonging to the I/i system. These are
oligosaccharides composed of repeated units of N:-acetyllactosamine, expressed
on RBC. The three-dimensional structure of the Fab of KAU, a human monoclonal
IgM CA with anti-I activity, was determined. The KAU combining site shows an
extended cavity and a neighboring pocket. Residues from the hypervariable loops
V(H)CDR3, V(L)CDR1, and V(L)CDR3 form the cavity, whereas the small pocket is
defined essentially by residues from the hypervariable loops V(H)CDR1 and
V(H)CDR2. This fact could explain the V(H)4-34 germline gene restriction among
CA. The KAU combining site topography is consistent with one that binds a
polysaccharide. The combining site overall dimensions are 15 A wide and 24 A
long. Conservation of key binding site residues among anti-I/i CAs indicates
that this is a common feature of this family of autoantibodies. We also describe
the first high resolution structure of the human IgM C(H)1:C(L) domain. The
structural analysis shows that the C(H)1-C(L) interface is mainly conserved
during the isotype switch process from IgM to IgG1.
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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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J.S.McLellan,
M.Pancera,
C.Carrico,
J.Gorman,
J.P.Julien,
R.Khayat,
R.Louder,
R.Pejchal,
M.Sastry,
K.Dai,
S.O'Dell,
N.Patel,
S.Shahzad-ul-Hussan,
Y.Yang,
B.Zhang,
T.Zhou,
J.Zhu,
J.C.Boyington,
G.Y.Chuang,
D.Diwanji,
I.Georgiev,
Y.D.Kwon,
D.Lee,
M.K.Louder,
S.Moquin,
S.D.Schmidt,
Z.Y.Yang,
M.Bonsignori,
J.A.Crump,
S.H.Kapiga,
N.E.Sam,
B.F.Haynes,
D.R.Burton,
W.C.Koff,
L.M.Walker,
S.Phogat,
R.Wyatt,
J.Orwenyo,
L.X.Wang,
J.Arthos,
C.A.Bewley,
J.R.Mascola,
G.J.Nabel,
W.R.Schief,
A.B.Ward,
I.A.Wilson,
and
P.D.Kwong
(2011).
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
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Nature,
480,
336-343.
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PDB codes:
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S.J.Thorpe,
C.Ball,
B.Fox,
K.M.Thompson,
R.Thorpe,
and
A.Bristow
(2008).
Anti-D and anti-i activities are inseparable in V4-34-encoded monoclonal anti-D: the same framework 1 residues are required for both reactivities.
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Transfusion,
48,
930-940.
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A.Conti,
P.Ricchiuto,
S.Iannaccone,
B.Sferrazza,
A.Cattaneo,
A.Bachi,
A.Reggiani,
M.Beltramo,
and
M.Alessio
(2005).
Pigment epithelium-derived factor is differentially expressed in peripheral neuropathies.
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Proteomics,
5,
4558-4567.
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P.A.Ramsland,
and
W.Farrugia
(2002).
Crystal structures of human antibodies: a detailed and unfinished tapestry of immunoglobulin gene products.
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J Mol Recognit,
15,
248-259.
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T.Dörner,
and
P.E.Lipsky
(2001).
Immunoglobulin variable-region gene usage in systemic autoimmune diseases.
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Arthritis Rheum,
44,
2715-2727.
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
