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PDBsum entry 1amc
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Proteinase inhibitor(trypsin)
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PDB id
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1amc
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DOI no:
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Biochemistry
33:7788-7796
(1994)
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PubMed id:
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Solution structure of residues 1-28 of the amyloid beta-peptide.
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J.Talafous,
K.J.Marcinowski,
G.Klopman,
M.G.Zagorski.
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ABSTRACT
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The three-dimensional solution structure of residues 1-28 of the amyloid
beta-peptide was determined using nuclear magnetic resonance spectroscopy,
distance geometry, and molecular dynamic techniques. The nuclear magnetic
resonance data used to derive the structure consisted of nuclear Overhauser
enhancements, vicinal coupling constants, and temperature coefficients of the
amide-NH chemical shifts. The beta-peptide is the major proteinaceous component
of amyloid deposits in Alzheimer's disease. In membrane-like media, the peptide
folds to form a predominately alpha-helical structure with a bend centered at
residue 12. The side chains of histidine-13 and lysine-16 are close, residing on
the same face of the helix. Their proximity may constitute a binding motif with
the heparan sulfate proteoglycans. The molecular details of the structure shown
here could facilitate the design of rational treatments to curtail the binding
of heparan sulfate proteoglycans or to prevent an alpha-helix-->beta-sheet
conversion that may occur during the early stages of amyloid formation in
Alzheimer's disease.
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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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E.Martineau,
J.M.de Guzman,
L.Rodionova,
X.Kong,
P.M.Mayer,
and
A.M.Aman
(2010).
Investigation of the noncovalent interactions between anti-amyloid agents and amyloid beta peptides by ESI-MS.
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J Am Soc Mass Spectrom,
21,
1506-1514.
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M.Valerio,
F.Porcelli,
J.P.Zbilut,
A.Giuliani,
C.Manetti,
and
F.Conti
(2008).
pH effects on the conformational preferences of amyloid beta-peptide (1-40) in HFIP aqueous solution by NMR spectroscopy.
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ChemMedChem,
3,
833-843.
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X.Dong,
W.Chen,
N.Mousseau,
and
P.Derreumaux
(2008).
Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).
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J Chem Phys,
128,
125108.
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J.Jarvet,
J.Danielsson,
P.Damberg,
M.Oleszczuk,
and
A.Gräslund
(2007).
Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes.
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J Biomol NMR,
39,
63-72.
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L.Li,
and
C.Hölscher
(2007).
Common pathological processes in Alzheimer disease and type 2 diabetes: a review.
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Brain Res Rev,
56,
384-402.
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N.A.Shirwany,
D.Payette,
J.Xie,
and
Q.Guo
(2007).
The amyloid beta ion channel hypothesis of Alzheimer's disease.
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Neuropsychiatr Dis Treat,
3,
597-612.
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S.Rodziewicz-Motowidło,
P.Juszczyk,
A.S.Kołodziejczyk,
E.Sikorska,
A.Skwierawska,
M.Oleszczuk,
and
Z.Grzonka
(2007).
Conformational solution studies of the SDS micelle-bound 11-28 fragment of two Alzheimer's beta-amyloid variants (E22K and A21G) using CD, NMR, and MD techniques.
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Biopolymers,
87,
23-39.
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P.K.Mandal,
J.W.Pettegrew,
D.W.McKeag,
and
R.Mandal
(2006).
Alzheimer's disease: halothane induces Abeta peptide to oligomeric form--solution NMR studies.
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Neurochem Res,
31,
883-890.
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S.Zirah,
S.A.Kozin,
A.K.Mazur,
A.Blond,
M.Cheminant,
I.Ségalas-Milazzo,
P.Debey,
and
S.Rebuffat
(2006).
Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.
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J Biol Chem,
281,
2151-2161.
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PDB codes:
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W.Chen,
N.Mousseau,
and
P.Derreumaux
(2006).
The conformations of the amyloid-beta (21-30) fragment can be described by three families in solution.
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J Chem Phys,
125,
084911.
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A.D.Ferrão-Gonzales,
B.K.Robbs,
V.H.Moreau,
A.Ferreira,
L.Juliano,
A.P.Valente,
F.C.Almeida,
J.L.Silva,
and
D.Foguel
(2005).
Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species.
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J Biol Chem,
280,
34747-34754.
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D.V.Laurents,
P.M.Gorman,
M.Guo,
M.Rico,
A.Chakrabartty,
and
M.Bruix
(2005).
Alzheimer's Abeta40 studied by NMR at low pH reveals that sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) binds and promotes beta-ball oligomerization.
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J Biol Chem,
280,
3675-3685.
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M.Valerio,
A.Colosimo,
F.Conti,
A.Giuliani,
A.Grottesi,
C.Manetti,
and
J.P.Zbilut
(2005).
Early events in protein aggregation: molecular flexibility and hydrophobicity/charge interaction in amyloid peptides as studied by molecular dynamics simulations.
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Proteins,
58,
110-118.
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S.C.Meredith
(2005).
Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins.
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Ann N Y Acad Sci,
1066,
181-221.
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A.Mukherjee,
and
B.Bagchi
(2004).
Contact pair dynamics during folding of two small proteins: chicken villin head piece and the Alzheimer protein beta-amyloid.
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J Chem Phys,
120,
1602-1612.
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C.Morgan,
M.Colombres,
M.T.Nuñez,
and
N.C.Inestrosa
(2004).
Structure and function of amyloid in Alzheimer's disease.
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Prog Neurobiol,
74,
323-349.
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G.Tiana,
F.Simona,
R.A.Broglia,
and
G.Colombo
(2004).
Thermodynamics of beta-amyloid fibril formation.
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J Chem Phys,
120,
8307-8317.
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J.Huang,
Y.Yao,
J.Lin,
Y.H.Ye,
W.Y.Sun,
and
W.X.Tang Dagger
(2004).
The solution structure of rat Abeta-(1-28) and its interaction with zinc ion: insights into the scarcity of amyloid deposition in aged rat brain.
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J Biol Inorg Chem,
9,
627-635.
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PDB code:
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A.Kapurniotu,
A.Buck,
M.Weber,
A.Schmauder,
T.Hirsch,
J.Bernhagen,
and
M.Tatarek-Nossol
(2003).
Conformational restriction via cyclization in beta-amyloid peptide Abeta(1-28) leads to an inhibitor of Abeta(1-28) amyloidogenesis and cytotoxicity.
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Chem Biol,
10,
149-159.
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R.M.Murphy
(2002).
Peptide aggregation in neurodegenerative disease.
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Annu Rev Biomed Eng,
4,
155-174.
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C.M.Yip,
and
J.McLaurin
(2001).
Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.
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Biophys J,
80,
1359-1371.
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E.Maioli,
C.Torricelli,
A.Santucci,
P.Martelli,
and
A.Pacini
(2001).
Plasma factors controlling atrial natriuretic peptide (ANP) aggregation: role of lipoproteins.
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Biochim Biophys Acta,
1536,
123-132.
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F.Massi,
and
J.E.Straub
(2001).
Probing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide.
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Biophys J,
81,
697-709.
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J.McLaurin,
and
P.E.Fraser
(2000).
Effect of amino-acid substitutions on Alzheimer's amyloid-beta peptide-glycosaminoglycan interactions.
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Eur J Biochem,
267,
6353-6361.
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L.C.Serpell
(2000).
Alzheimer's amyloid fibrils: structure and assembly.
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Biochim Biophys Acta,
1502,
16-30.
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Y.Bourne,
P.Taylor,
P.E.Bougis,
and
P.Marchot
(1999).
Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.
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J Biol Chem,
274,
2963-2970.
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PDB code:
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D.B.Teplow
(1998).
Structural and kinetic features of amyloid beta-protein fibrillogenesis.
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Amyloid,
5,
121-142.
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M.Coles,
W.Bicknell,
A.A.Watson,
D.P.Fairlie,
and
D.J.Craik
(1998).
Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
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Biochemistry,
37,
11064-11077.
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PDB code:
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C.D.Kroenke,
D.Ziemnicka-Kotula,
J.Xu,
L.Kotula,
and
A.G.Palmer
(1997).
Solution conformations of a peptide containing the cytoplasmic domain sequence of the beta amyloid precursor protein.
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Biochemistry,
36,
8145-8152.
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T.G.Fletcher,
and
D.A.Keire
(1997).
The interaction of beta-amyloid protein fragment (12-28) with lipid environments.
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Protein Sci,
6,
666-675.
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A.R.Salomon,
K.J.Marcinowski,
R.P.Friedland,
and
M.G.Zagorski
(1996).
Nicotine inhibits amyloid formation by the beta-peptide.
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Biochemistry,
35,
13568-13578.
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B.Solomon,
R.Koppel,
E.Hanan,
and
T.Katzav
(1996).
Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide.
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Proc Natl Acad Sci U S A,
93,
452-455.
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J.E.Maggio,
and
P.W.Mantyh
(1996).
Brain amyloid--a physicochemical perspective.
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Brain Pathol,
6,
147-162.
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T.Kohno,
K.Kobayashi,
T.Maeda,
K.Sato,
and
A.Takashima
(1996).
Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment.
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Biochemistry,
35,
16094-16104.
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PDB code:
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W.P.Esler,
E.R.Stimson,
J.R.Ghilardi,
H.V.Vinters,
J.P.Lee,
P.W.Mantyh,
and
J.E.Maggio
(1996).
In vitro growth of Alzheimer's disease beta-amyloid plaques displays first-order kinetics.
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Biochemistry,
35,
749-757.
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A.L.Schwarzman,
L.Gregori,
M.P.Vitek,
S.Lyubski,
W.J.Strittmatter,
J.J.Enghilde,
R.Bhasin,
J.Silverman,
K.H.Weisgraber,
and
P.K.Coyle
(1994).
Transthyretin sequesters amyloid beta protein and prevents amyloid formation.
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Proc Natl Acad Sci U S A,
91,
8368-8372.
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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
