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PDBsum entry 1x9p
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Virus like particle
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PDB id
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1x9p
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References listed in PDB file
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Key reference
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Title
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The structure of the human adenovirus 2 penton.
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Authors
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C.Zubieta,
G.Schoehn,
J.Chroboczek,
S.Cusack.
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Ref.
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Mol Cell, 2005,
17,
121-135.
[DOI no: ]
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PubMed id
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Abstract
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The adenovirus penton, a noncovalent complex of the pentameric penton base and
trimeric fiber proteins, comprises the vertices of the adenovirus capsid and
contains all necessary components for viral attachment and internalization. The
3.3 A resolution crystal structure of human adenovirus 2 (hAd2) penton base
shows that the monomer has a basal jellyroll domain and a distal irregular
domain formed by two long insertions, a similar topology to the adenovirus
hexon. The Arg-Gly-Asp (RGD) motif, required for interactions with cellular
integrins, occurs on a flexible surface loop. The complex of penton base with
bound N-terminal fiber peptide, determined at 3.5 A resolution, shows that the
universal fiber motif FNPVYPY binds at the interface of adjacent penton base
monomers and results in a localized structural rearrangement in the insertion
domain of the penton base. These results give insight into the structure and
assembly of the adenovirus capsid and will be of use for gene-therapy
applications.
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Figure 3.
Figure 3. Structure of the Adenovirus 2 Penton Base(A)
Left, tricolor ribbon representation of the monomer with the
jellyroll domain (green) and the insertion domain (blue,
residues 129–434; red, residues 466–519). The termini are
labeled N and C. The variable loop and the RGD loop are labeled
with disordered residues 298–373 of the RGD loop depicted by a
dotted line. Putative zwittergent 3-12 molecules are drawn as
stick representations. Right, rainbow ribbon representation
colored from N terminus (blue) to C terminus (red) viewed after
rotation of approximately 90° from previous image.(B) Stereo
view of the putative zwittergent 3-12 binding site on the penton
base monomer. The detergent molecules are colored green.
Interacting residues from the protein are cyan.(C) The pentamer,
the functional unit of the penton base protein, shown as a
surface representation (left) and ribbon diagram (right), with
each monomer colored uniquely. The variable loop, RGD loop and
N- and C termini are marked.
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Figure 4.
Figure 4. Fiber Peptide Interactions with the Penton
Base(A) Stereo diagram of the fiber peptide (red) bound to the
penton base subunit interface viewed looking down the 5-fold
axis.(B) Stereo view of the peptide binding site. The ribbon
diagrams of the monomers are colored blue and green and the
bound peptide is depicted as sticks with carbons colored white.
Residues forming the peptide binding pocket are colored yellow
for monomer A and orange for monomer B. Putative hydrogen
bonding interactions are denoted by dashed yellow lines.(C)
Stereo view of the experimental averaged electron density of the
bound peptide.(D) Sequence alignment of the N-terminal portion
of representative fiber proteins from serotypes Ad2, accession
number P03275; Ad3, P04501; Ad7, AAR89975; Ad11, NP_852715;
Ad12, DAA00575; Ad17, DAA00599; Ad25, NP_478420; Ad37, AAB71734;
Ad41 short fiber, P16883; and Ad41 long fiber, P14267. Conserved
residues (yellow) and the peptide sequence used for structural
analysis (red) are highlighted.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2005,
17,
121-135)
copyright 2005.
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