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PDBsum entry 2vzi
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Cell adhesion
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PDB id
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2vzi
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References listed in PDB file
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Key reference
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Title
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Structural analysis of the interactions between paxillin ld motifs and alpha-Parvin.
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Authors
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S.Lorenz,
I.Vakonakis,
E.D.Lowe,
I.D.Campbell,
M.E.Noble,
M.K.Hoellerer.
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Ref.
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Structure, 2008,
16,
1521-1531.
[DOI no: ]
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PubMed id
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Abstract
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The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs
that interact with a variety of focal adhesion proteins, such as alpha-parvin.
Here, we report the first crystal structure of the C-terminal calponin homology
domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to
bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal
structures with these LD motifs reveal the molecular details of their
interactions with a common binding site on alpha-parvin-CH(C), which is located
at the rim of the canonical fold and includes part of the inter-CH domain
linker. Surprisingly, this binding site can accommodate LD motifs in two
antiparallel orientations. Taken together, these results reveal an unusual
degree of binding degeneracy in the paxillin/alpha-parvin system that may
facilitate the assembly of dynamic signaling complexes in the cell.
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Figure 4.
Figure 4. Cocrystal Structure of α-Parvin-CH[C] with
Paxillin LD1
Superposition of the ribbon representations of
α-parvin-CH[C] in blue and its complex with the LD1 peptide in
gold and green, respectively. Secondary structural elements are
indicated.
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Figure 5.
Figure 5. PRE Experiment with Spin-Labeled LD1
(A)
Details of the ^1H-^15N HSQC spectra of 230 μM ^15N-enriched
α-parvin-CH[C] and 250 μM PROXYL-labeled LD1 peptide in the
absence (left) and presence (right) of 5 mM ascorbate. The
latter serves to reduce the spin label, thereby eliminating PRE
effects. The binding orientation of LD1 seen in the crystal
structure is denoted “forward.”
(B) Ribbon
representation of α-parvin-CH[C] in gold and LD1 in green. The
position of α-parvin residues 257 and 370 are highlighted in
blue and red, respectively.
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The above figures are
reprinted
from an Open Access publication published by Cell Press:
Structure
(2008,
16,
1521-1531)
copyright 2008.
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