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PDBsum entry 1g47
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Cell adhesion
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PDB id
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1g47
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of the focal adhesion adaptor pinch lim1 domain and characterization of its interaction with the integrin-Linked kinase ankyrin repeat domain.
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Authors
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A.Velyvis,
Y.Yang,
C.Wu,
J.Qin.
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Ref.
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J Biol Chem, 2001,
276,
4932-4939.
[DOI no: ]
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PubMed id
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Abstract
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PINCH is a recently identified adaptor protein that comprises an array of five
LIM domains. PINCH functions through LIM-mediated protein-protein interactions
that are involved in cell adhesion, growth, and differentiation. The LIM1 domain
of PINCH interacts with integrin-linked kinase (ILK), thereby mediating focal
adhesions via a specific integrin/ILK signaling pathway. We have solved the NMR
structure of the PINCH LIM1 domain and characterized its binding to ILK. LIM1
contains two contiguous zinc fingers of the CCHC and CCCH types and adopts a
global fold similar to that of functionally distinct LIM domains from
cysteine-rich protein and cysteine-rich intestinal protein families with CCHC
and CCCC zinc finger types. Gel-filtration and NMR experiments demonstrated a
1:1 complex between PINCH LIM1 and the ankyrin repeat domain of ILK. A chemical
shift mapping experiment identified regions in PINCH LIM1 that are important for
interaction with ILK. Comparison of surface features between PINCH LIM1 and
other functionally different LIM domains indicated that the LIM motif might have
a highly variable mode in recognizing various target proteins.
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Figure 1.
Fig. 1. Alignment of amino acid sequences of LIM domains
with known structures. Alignment was generated with BLAST
Version 2.0 (37). Sequence numbering is that of the PINCH
protein. Highlighted in black are Zn2+-coordinating residues.
The Lasp-1 structure comprises only the first zinc finger, half
of the LIM domain. The structure with Protein Data Bank (PDB)
code 1cxx is the R122A mutant of qCRP2 LIM2. cCRP1, chicken CRP1.
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Figure 3.
Fig. 3. Hydrophobic features of the PINCH LIM1 domain. A,
side chain arrangement of hydrophobic core residues of the
average minimized structure of PINCH LIM1; B, hydrophobic patch
residues near the C terminus of the average minimized structure.
The thin ribbon represents the backbone of residues 49-67 (  -sheet 4 and
 -helix);
side chains are shown as sticks.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
4932-4939)
copyright 2001.
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