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PDBsum entry 2m32
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Cell adhesion
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PDB id
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2m32
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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 integrin α1i domain in complex with a collagen-Mimetic peptide.
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Authors
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Y.K.Chin,
S.J.Headey,
B.Mohanty,
R.Patil,
P.A.Mcewan,
J.D.Swarbrick,
T.D.Mulhern,
J.Emsley,
J.S.Simpson,
M.J.Scanlon.
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Ref.
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J Biol Chem, 2013,
288,
36796-36809.
[DOI no: ]
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PubMed id
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Abstract
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We have determined the structure of the human integrin α1I domain bound to a
triple-helical collagen peptide. The structure of the α1I-peptide complex was
investigated using data from NMR, small angle x-ray scattering, and size
exclusion chromatography that were used to generate and validate a model of the
complex using the data-driven docking program, HADDOCK (High Ambiguity Driven
Biomolecular Docking). The structure revealed that the α1I domain undergoes a
major conformational change upon binding of the collagen peptide. This involves
a large movement in the C-terminal helix of the αI domain that has been
suggested to be the mechanism by which signals are propagated in the intact
integrin receptor. The structure suggests a basis for the different binding
selectivity observed for the α1I and α2I domains. Mutational data identify
residues that contribute to the conformational change observed. Furthermore,
small angle x-ray scattering data suggest that at low collagen peptide
concentrations the complex exists in equilibrium between a 1:1 and 2:1
α1I-peptide complex.
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