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PDBsum entry 3f6q
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Signaling protein/signaling protein
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PDB id
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3f6q
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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 structural basis of integrin-Linked kinase-Pinch interactions.
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Authors
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B.P.Chiswell,
R.Zhang,
J.W.Murphy,
T.J.Boggon,
D.A.Calderwood.
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Ref.
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Proc Natl Acad Sci U S A, 2008,
105,
20677-20682.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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The heterotrimeric complex between integrin-linked kinase (ILK), PINCH, and
parvin is an essential signaling platform, serving as a convergence point for
integrin and growth-factor signaling and regulating cell adhesion, spreading,
and migration. We report a 1.6-A crystal structure of the ILK ankyrin repeat
domain bound to the PINCH1 LIM1 domain, revealing the molecular basis of
ILK-PINCH interactions and providing a structural description of this region of
ILK. This structure identifies 5 ankyrin repeats in ILK, explains previous
deletion mutagenesis data, permits identification of ILK and PINCH1 point
mutations that disrupt the interaction, shows how zincs are coordinated by
PINCH1 LIM1, and suggests that conformational flexibility and twisting between
the 2 zinc fingers within the LIM1 domain may be important for ILK binding.
These data provide an atomic-resolution description of a key interaction in the
ILK-PINCH-parvin scaffolding complex.
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Figure 1.
Structure of the ILK ANK repeat domain in complex with PINCH
LIM1. (A) Schematic showing the domains of ILK and PINCH. (B)
Cartoon of the structure of the LIM1 domain of PINCH1 in complex
with ILK. PINCH1 is shown in light green with zincs as yellow
spheres and the vector-derived N-terminal β-strand (strand
−z) in light blue. ILK is colored according to ANK repeat
(ANK1 yellow; ANK2 red; ANK3 green; ANK4 purple; ANK5 blue).
This color scheme is maintained throughout the manuscript. (C)
Example 2F[o]-F[c] electron density maps contoured at 1.5 σ.
Clear density for ILK residues Tyr-106 and Trp-110 is visible.
All figures are made by using PYMOL (www.pymol.org).
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Figure 4.
Architecture of the interaction. (Center) Illustration of a
top-view schematic of the ILK interaction with PINCH1. Three
views show this interaction from different angles. (Left) Toward
PINCH1 (gray surface) from the ILK ANK repeat finger side of the
interaction. Lower images are toward PINCH1 (gray surface) from
the ILK ANK repeat palm side of the interaction. (Right) Toward
ILK (gray surface). Shown in red is PINCH1 backbone trace.
Blown-up views show labels for residues involved in the
interaction.
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