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PDBsum entry 4bjl
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Immunoglobulin
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PDB id
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4bjl
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Contents |
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* Residue conservation analysis
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Proc Natl Acad Sci U S A
93:7017-7021
(1996)
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PubMed id:
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Three quaternary structures for a single protein.
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D.B.Huang,
C.F.Ainsworth,
F.J.Stevens,
M.Schiffer.
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ABSTRACT
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The structure of a multisubunit protein (immunoglobulin light chain) was solved
in three crystal forms, differing only in the solvent of crystallization. The
three structures were obtained at high ionic strength and low pH, high ionic
strength and high pH, and low ionic strength and neutral pH. The three resulting
"snapshots" of possible structures show that their variable-domain interactions
differ, reflecting their stabilities under specific solvent conditions. In the
three crystal forms, the variable domains had different rotational and
translational relationships, whereas no alteration of the constant domains was
found. The critical residues involved in the observed effect of the solvent are
tryptophans and histidines located between the two variable domains in the
dimeric structure. Tryptophan residues are commonly found in interfaces between
proteins and their subunits, and histidines have been implicated in pH-dependent
conformation changes. The quaternary structure observed for a multisubunit
protein or protein complex in a crystal may be influenced by the interactions of
the constituents within the molecule or complex and/or by crystal packing
interactions. The comparison of buried surface areas and hydrogen bonds between
the domains forming the molecule and between the molecules forming the crystals
suggest that, for this system, the interactions within the molecule are most
likely the determining factors.
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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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A.M.Gronenborn
(2009).
Protein acrobatics in pairs--dimerization via domain swapping.
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Curr Opin Struct Biol,
19,
39-49.
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K.S.Keating,
S.C.Flores,
M.B.Gerstein,
and
L.A.Kuhn
(2009).
StoneHinge: hinge prediction by network analysis of individual protein structures.
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Protein Sci,
18,
359-371.
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V.Sharma,
W.Heriot,
K.Trisler,
and
V.Smider
(2009).
A human germ line antibody light chain with hydrolytic properties associated with multimerization status.
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J Biol Chem,
284,
33079-33087.
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D.L.Makino,
A.H.Henschen-Edman,
S.B.Larson,
and
A.McPherson
(2007).
Bence Jones KWR protein structures determined by X-ray crystallography.
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Acta Crystallogr D Biol Crystallogr,
63,
780-792.
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PDB codes:
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D.L.Makino,
A.H.Henschen-Edman,
and
A.McPherson
(2005).
Four crystal forms of a Bence-Jones protein.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
79-82.
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M.Król,
I.Roterman,
B.Piekarska,
L.Konieczny,
J.Rybarska,
B.Stopa,
P.Spólnik,
and
E.Szneler
(2005).
An approach to understand the complexation of supramolecular dye Congo red with immunoglobulin L chain lambda.
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Biopolymers,
77,
155-162.
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M.Król,
I.Roterman,
B.Piekarska,
L.Konieczny,
J.Rybarska,
B.Stopa,
and
P.Spólnik
(2005).
Analysis of correlated domain motions in IgG light chain reveals possible mechanisms of immunological signal transduction.
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Proteins,
59,
545-554.
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L.Cao,
L.Langen,
and
R.A.Sheldon
(2003).
Immobilised enzymes: carrier-bound or carrier-free?
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Curr Opin Biotechnol,
14,
387-394.
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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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B.Piekarska,
L.Konieczny,
J.Rybarska,
B.Stopa,
G.Zemanek,
E.Szneler,
M.Król,
M.Nowak,
and
I.Roterman
(2001).
Heat-induced formation of a specific binding site for self-assembled Congo Red in the V domain of immunoglobulin L chain lambda.
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Biopolymers,
59,
446-456.
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T.C.Mueser,
P.H.Rogers,
and
A.Arnone
(2000).
Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin.
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Biochemistry,
39,
15353-15364.
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PDB codes:
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P.R.Pokkuluri,
A.Solomon,
D.T.Weiss,
F.J.Stevens,
and
M.Schiffer
(1999).
Tertiary structure of human lambda 6 light chains.
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Amyloid,
6,
165-171.
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PDB codes:
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P.R.Pokkuluri,
D.B.Huang,
R.Raffen,
X.Cai,
G.Johnson,
P.W.Stevens,
F.J.Stevens,
and
M.Schiffer
(1998).
A domain flip as a result of a single amino-acid substitution.
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Structure,
6,
1067-1073.
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PDB codes:
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S.Kim,
and
B.A.Barry
(1998).
Vibrational spectrum associated with the reduction of tyrosyl radical D* in photosystem II: a comparative biochemical and kinetic study.
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Biochemistry,
37,
13882-13892.
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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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