Biophysical analysis of Kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif.

doi:10.1074/jbc.M112.415208

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Article

Biophysical analysis of Kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif.

The Journal of biological chemistry - 2 Nov 2012

Yates Luke A, Füzéry Anna K, Bonet Roman, Campbell Iain D, Gilbert Robert J C

Abstract excerpt

Kindlin-3, a 75-kDa protein, has been shown to be critical for hemostasis, immunity, and bone metabolism via its role in integrin activation. The Kindlin family is hallmarked by a FERM domain comprised of F1, F2, and F3 subdomains together with an N-terminal F0 domain and a pleckstrin homology domain inserted in the F2 domain. Recombinant Kindlin-3 was cloned, expressed, and purified, and its domain organization...

Topics

Amino Acid Motifs
Amino Acid Sequence
Animals
Biophysical Phenomena
Cytoskeletal Proteins
Integrin beta1
Magnetic Resonance Spectroscopy
Membrane Proteins
Mice
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Conformation

Protein Isoforms

Protein Structure, Tertiary

Protein Subunits

Recombinant Proteins

Scattering, Small Angle

Sf9 Cells

Source

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Identifiers

PMID: 22989875
DOI: 10.1074/jbc.M112.415208
PMCID: PMC3488048

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