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PDBsum entry 1nim
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Fimbrial protein
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PDB id
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1nim
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PDB id:
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Fimbrial protein
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Title:
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A comparison of nmr solution structures of the receptor binding domains of pseudomonas aeruginosa pili strains pao, kb7, and pak: implications for receptor binding and synthetic vaccine design
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Structure:
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Pak pilin, trans. Chain: a. Synonym: fimbrial protein. Engineered: yes
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Source:
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Pseudomonas aeruginosa. Organism_taxid: 287. Strain: k
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NMR struc:
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25 models
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Authors:
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A.P.Campbell,C.Mcinnes,R.S.Hodges,B.D.Sykes
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Key ref:
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A.P.Campbell
et al.
(1995).
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.
Biochemistry,
34,
16255-16268.
PubMed id:
DOI:
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Date:
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05-Oct-95
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Release date:
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29-Jan-96
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PROCHECK
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Headers
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References
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P02973
(FMPA_PSEAI) -
Fimbrial protein from Pseudomonas aeruginosa
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Seq:
Struc:
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150 a.a.
17 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Biochemistry
34:16255-16268
(1995)
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PubMed id:
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Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.
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A.P.Campbell,
C.McInnes,
R.S.Hodges,
B.D.Sykes.
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ABSTRACT
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The solution structures of peptide antigens from the receptor binding domains of
Pseudomonas aeruginosa strains PAO and KB7 have been determined using
two-dimensional 1H NMR techniques. Ensembles of solution conformations for the
trans forms of these 17-residue disulfide-bridged peptides have been generated
using a simulated annealing procedure in conjunction with distance and torsion
angle restraints derived from NMR data. Comparison of the NMR-derived solution
structures of the PAO and KB7 peptides, with that previously determined (McInnes
et al., 1993) and herein refined for the PAK peptide reveals a common structural
motif. All three peptide structures contain a type I beta-turn in the conserved
sequence Asp134-X-X-Phe137 and a type II beta-turn in the conserved sequence
Pro139-X-Gly-Cys142. However, the overall folds of the three peptides differ as
well as the disposition of the side chains comprising the hydrophobic pockets.
The similarities and differences between the structures of the three strains
which bind to a common cell surface receptor are discussed in light of their
contributions to synthetic vaccine design.
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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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C.Hackbarth,
and
R.S.Hodges
(2010).
Synthetic peptide vaccine development: designing dual epitopes into a single pilin peptide immunogen generates antibody cross-reactivity between two strains of Pseudomonas aeruginosa.
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Chem Biol Drug Des,
76,
293-304.
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D.J.Kao,
and
R.S.Hodges
(2009).
Advantages of a synthetic peptide immunogen over a protein immunogen in the development of an anti-pilus vaccine for Pseudomonas aeruginosa.
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Chem Biol Drug Des,
74,
33-42.
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H.Harvey,
M.Habash,
F.Aidoo,
and
L.L.Burrows
(2009).
Single-residue changes in the C-terminal disulfide-bonded loop of the Pseudomonas aeruginosa type IV pilin influence pilus assembly and twitching motility.
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J Bacteriol,
191,
6513-6524.
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C.L.Giltner,
E.J.van Schaik,
G.F.Audette,
D.Kao,
R.S.Hodges,
D.J.Hassett,
and
R.T.Irvin
(2006).
The Pseudomonas aeruginosa type IV pilin receptor binding domain functions as an adhesin for both biotic and abiotic surfaces.
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Mol Microbiol,
59,
1083-1096.
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T.Murata,
H.Hemmi,
S.Nakamura,
K.Shimizu,
Y.Suzuki,
and
I.Yamaguchi
(2005).
Structure, epitope mapping, and docking simulation of a gibberellin mimic peptide as a peptidyl mimotope for a hydrophobic ligand.
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FEBS J,
272,
4938-4948.
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PDB code:
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P.J.Cachia,
D.J.Kao,
and
R.S.Hodges
(2004).
Synthetic peptide vaccine development: measurement of polyclonal antibody affinity and cross-reactivity using a new peptide capture and release system for surface plasmon resonance spectroscopy.
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J Mol Recognit,
17,
540-557.
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X.F.Xu,
Y.W.Tan,
L.Lam,
J.Hackett,
M.Zhang,
and
Y.K.Mok
(2004).
NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
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J Biol Chem,
279,
31599-31605.
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PDB code:
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J.Schuman,
A.P.Campbell,
R.R.Koganty,
and
B.M.Longenecker
(2003).
Probing the conformational and dynamical effects of O-glycosylation within the immunodominant region of a MUC1 peptide tumor antigen.
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J Pept Res,
61,
91.
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M.A.Johnson,
M.Jaseja,
W.Zou,
H.J.Jennings,
V.Copie,
B.M.Pinto,
and
S.H.Pincus
(2003).
NMR studies of carbohydrates and carbohydrate-mimetic peptides recognized by an anti-group B Streptococcus antibody.
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J Biol Chem,
278,
24740-24752.
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P.J.Cachia,
and
R.S.Hodges
(2003).
Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa.
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Biopolymers,
71,
141-168.
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J.S.Grinstead,
R.R.Koganty,
M.J.Krantz,
B.M.Longenecker,
and
A.P.Campbell
(2002).
Effect of glycosylation on MUC1 humoral immune recognition: NMR studies of MUC1 glycopeptide-antibody interactions.
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Biochemistry,
41,
9946-9961.
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M.Katragadda,
J.L.Alderfer,
and
P.L.Yeagle
(2001).
Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin.
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Biophys J,
81,
1029-1036.
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PDB code:
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A.P.Campbell,
W.Y.Wong,
R.T.Irvin,
and
B.D.Sykes
(2000).
Interaction of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK with a cross-reactive antibody: conformation of the bound peptide.
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Biochemistry,
39,
14847-14864.
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D.Morikis,
N.Assa-Munt,
A.Sahu,
and
J.D.Lambris
(1998).
Solution structure of Compstatin, a potent complement inhibitor.
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Protein Sci,
7,
619-627.
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PDB code:
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M.A.Molins,
M.A.Contreras,
I.Fita,
and
M.Pons
(1998).
Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti-HRV2 neutralizing antibody.
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J Pept Sci,
4,
101-110.
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A.P.Campbell,
D.L.Bautista,
B.Tripet,
W.Y.Wong,
R.T.Irvin,
R.S.Hodges,
and
B.D.Sykes
(1997).
Solution secondary structure of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pili strain PAK: A heteronuclear multidimensional NMR study.
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Biochemistry,
36,
12791-12801.
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D.H.Jones,
R.S.Hodges,
K.R.Barber,
and
C.W.Grant
(1997).
Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
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Protein Sci,
6,
2459-2461.
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P.L.Yeagle,
J.L.Alderfer,
and
A.D.Albert
(1997).
Three-dimensional structure of the cytoplasmic face of the G protein receptor rhodopsin.
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Biochemistry,
36,
9649-9654.
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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
code is
shown on the right.
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Links
