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PDBsum entry 1z1y
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Cell adhesion
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PDB id
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1z1y
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Contents |
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* Residue conservation analysis
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PDB id:
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Cell adhesion
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Title:
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Crystal structure of methylated pvs25, an ookinete protein from plasmodium vivax
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Structure:
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Ookinete surface protein pvs25. Chain: a, b. Engineered: yes
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Source:
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Plasmodium vivax. Malaria parasite p. Vivax. Organism_taxid: 5855. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
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Resolution:
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2.00Å
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R-factor:
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0.245
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R-free:
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0.276
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Authors:
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A.K.Saxena,K.Singh,H.P.Su,M.M.Klein,A.W.Stowers,A.J.Saul,C.A.Long, D.N.Garboczi
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Key ref:
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A.K.Saxena
et al.
(2006).
The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms.
Nat Struct Mol Biol,
13,
90-91.
PubMed id:
DOI:
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Date:
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07-Mar-05
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Release date:
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06-Dec-05
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PROCHECK
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Headers
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References
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O96555
(O96555_PLAVI) -
Ookinete surface protein from Plasmodium vivax
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Seq: Struc:
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219 a.a.
177 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 22 residue positions (black
crosses)
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DOI no:
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Nat Struct Mol Biol
13:90-91
(2006)
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PubMed id:
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The essential mosquito-stage P25 and P28 proteins from Plasmodium form tile-like triangular prisms.
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A.K.Saxena,
K.Singh,
H.P.Su,
M.M.Klein,
A.W.Stowers,
A.J.Saul,
C.A.Long,
D.N.Garboczi.
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ABSTRACT
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P25 and P28 proteins are essential for Plasmodium parasites to infect mosquitoes
and are leading candidates for a transmission-blocking malaria vaccine. The
Plasmodium vivax P25 is a triangular prism that could tile the parasite surface.
The residues forming the triangle are conserved in P25 and P28 from all
Plasmodium species. A cocrystal structure shows that a transmission-blocking
antibody uses only its heavy chain to bind Pvs25 at a vertex of the triangle.
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Selected figure(s)
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Figure 1.
Figure 1. Views of Pvs25. (a) The triangular prism formed by
domain 1 (light blue), domain 2 (green), domain 3 (red) and
domain 4 (gold). The central -strands
in each domain are labeled 1 and 2. The 11 disulfide bonds
(violet) are shown. (b) View of the edge of the prism. (c) Pvs25
forms sheets in the crystals. One molecule (red) makes contacts
with four 2[1] symmetry mates (light blue) and two molecules
related by lattice translations (dark blue). The six light blue
molecules all have the same triangular face 'up', whereas the
other three molecules (red and dark blue) all have the opposite
face 'up'. As P25 and P28 molecules are thin prisms, the
glycosylphosphatidylinositol anchor could reach the cell
membrane whether a molecule was facing 'up' or 'down' on the
membrane. N term, N terminus; C term, C terminus.
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Figure 2.
Figure 2. Binding of transmission-blocking antibodies to Pvs25.
(a) 2A8 Fab bound via its heavy chain (dark blue) to the B
loop of Pvs25 domain 2. The light chain (light blue) does not
contact Pvs25. The B loop of Pvs25 domain 3 (red) extends up
from the plane of the triangle. (b) Monoclonal antibodies 1H10
and 1A5 do not bind in the presence of prebound 2A8. With Pvs25
immobilized on a Biacore chip, 2A8 was injected at (i) until
binding was saturated at (ii), and then the second antibody and
2A8 were injected at (iii) until (iv). Buffer without protein
was injected from (ii) to (iii) and from (iv) onward.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2006,
13,
90-91)
copyright 2006.
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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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T.Miyata,
T.Harakuni,
T.Tsuboi,
J.Sattabongkot,
H.Kohama,
M.Tachibana,
G.Matsuzaki,
M.Torii,
and
T.Arakawa
(2010).
Plasmodium vivax ookinete surface protein Pvs25 linked to cholera toxin B subunit induces potent transmission-blocking immunity by intranasal as well as subcutaneous immunization.
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Infect Immun,
78,
3773-3782.
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B.Sharma,
and
M.K.Jaiswal
(2009).
EGF domain II of protein Pb28 from Plasmodium berghei interacts with monoclonal transmission blocking antibody 13.1.
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J Mol Model,
15,
369-382.
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B.Sharma,
and
R.D.Ambedkar
(2009).
A very large C-loop in EGF domain IV is characteristic of the P28 family of ookinete surface proteins.
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J Mol Model,
15,
309-321.
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R.M.Couñago,
M.Davlieva,
U.Strych,
R.E.Hill,
and
K.L.Krause
(2009).
Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames).
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BMC Struct Biol,
9,
53.
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PDB code:
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P.R.Gilson,
R.A.O'Donnell,
T.Nebl,
P.R.Sanders,
M.E.Wickham,
T.F.McElwain,
T.F.de Koning-Ward,
and
B.S.Crabb
(2008).
MSP1(19) miniproteins can serve as targets for invasion inhibitory antibodies in Plasmodium falciparum provided they contain the correct domains for cell surface trafficking.
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Mol Microbiol,
68,
124-138.
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P.Srinivasan,
H.Fujioka,
and
M.Jacobs-Lorena
(2008).
PbCap380, a novel oocyst capsule protein, is essential for malaria parasite survival in the mosquito.
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Cell Microbiol,
10,
1304-1312.
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A.K.Saxena,
Y.Wu,
and
D.N.Garboczi
(2007).
Plasmodium p25 and p28 surface proteins: potential transmission-blocking vaccines.
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Eukaryot Cell,
6,
1260-1265.
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A.Saul
(2007).
Mosquito stage, transmission blocking vaccines for malaria.
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Curr Opin Infect Dis,
20,
476-481.
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K.Miura,
D.B.Keister,
O.V.Muratova,
J.Sattabongkot,
C.A.Long,
and
A.Saul
(2007).
Transmission-blocking activity induced by malaria vaccine candidates Pfs25/Pvs25 is a direct and predictable function of antibody titer.
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Malar J,
6,
107.
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P.Gayathri,
H.Balaram,
and
M.R.Murthy
(2007).
Structural biology of plasmodial proteins.
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Curr Opin Struct Biol,
17,
744-754.
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R.L.Rich,
and
D.G.Myszka
(2007).
Survey of the year 2006 commercial optical biosensor literature.
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J Mol Recognit,
20,
300-366.
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G.A.Bentley
(2006).
Functional and immunological insights from the three-dimensional structures of Plasmodium surface proteins.
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Curr Opin Microbiol,
9,
395-400.
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J.Huang,
and
W.Honda
(2006).
CED: a conformational epitope database.
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BMC Immunol,
7,
7.
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T.S.Walter,
C.Meier,
R.Assenberg,
K.F.Au,
J.Ren,
A.Verma,
J.E.Nettleship,
R.J.Owens,
D.I.Stuart,
and
J.M.Grimes
(2006).
Lysine methylation as a routine rescue strategy for protein crystallization.
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Structure,
14,
1617-1622.
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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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}
}
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