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PDBsum entry 3l1e
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* Residue conservation analysis
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Protein Sci
19:1031-1043
(2010)
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PubMed id:
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Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function.
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A.Laganowsky,
J.L.Benesch,
M.Landau,
L.Ding,
M.R.Sawaya,
D.Cascio,
Q.Huang,
C.V.Robinson,
J.Horwitz,
D.Eisenberg.
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ABSTRACT
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Small heat shock proteins alphaA and alphaB crystallin form highly polydisperse
oligomers that frustrate protein aggregation, crystallization, and amyloid
formation. Here, we present the crystal structures of truncated forms of bovine
alphaA crystallin (AAC(59-163)) and human alphaB crystallin (ABC(68-162)), both
containing the C-terminal extension that functions in chaperone action and
oligomeric assembly. In both structures, the C-terminal extensions swap into
neighboring molecules, creating runaway domain swaps. This interface, termed DS,
enables crystallin polydispersity because the C-terminal extension is
palindromic and thereby allows the formation of equivalent residue interactions
in both directions. That is, we observe that the extension binds in opposite
directions at the DS interfaces of AAC(59-163) and ABC(68-162). A second dimeric
interface, termed AP, also enables polydispersity by forming an antiparallel
beta sheet with three distinct registration shifts. These two polymorphic
interfaces enforce polydispersity of alpha crystallin. This evolved
polydispersity suggests molecular mechanisms for chaperone action and for
prevention of crystallization, both necessary for transparency of eye lenses.
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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.R.Clark,
C.E.Naylor,
C.Bagnéris,
N.H.Keep,
and
C.Slingsby
(2011).
Crystal structure of R120G disease mutant of human αB-crystallin domain dimer shows closure of a groove.
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J Mol Biol,
408,
118-134.
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PDB codes:
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E.Hilario,
F.J.Martin,
M.C.Bertolini,
and
L.Fan
(2011).
Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer.
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J Mol Biol,
408,
74-86.
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PDB codes:
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K.Takeda,
T.Hayashi,
T.Abe,
Y.Hirano,
Y.Hanazono,
M.Yohda,
and
K.Miki
(2011).
Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0.
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J Struct Biol,
174,
92-99.
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PDB codes:
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M.Raju,
P.Santhoshkumar,
T.M.Henzl,
and
K.K.Sharma
(2011).
Identification and characterization of a copper-binding site in αA-crystallin.
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Free Radic Biol Med,
50,
1429-1436.
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P.R.Banerjee,
A.Pande,
J.Patrosz,
G.M.Thurston,
and
J.Pande
(2011).
Cataract-associated mutant E107A of human gammaD-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering.
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Proc Natl Acad Sci U S A,
108,
574-579.
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S.Jehle,
B.S.Vollmar,
B.Bardiaux,
K.K.Dove,
P.Rajagopal,
T.Gonen,
H.Oschkinat,
and
R.E.Klevit
(2011).
N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity.
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Proc Natl Acad Sci U S A,
108,
6409-6414.
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S.Karmakar,
and
K.P.Das
(2011).
Stabilization of oligomeric structure of α-crystallin by Zn(+2) through intersubunit bridging.
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Biopolymers,
95,
105-116.
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A.Laganowsky,
and
D.Eisenberg
(2010).
Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin.
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Protein Sci,
19,
1978-1984.
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PDB code:
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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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