Integrin binding immunoglobulin type filamin domains have variable stability.

Journal article

Filamin, a large modular protein composed mainly of many immunoglobulin-like domains, is a potent cross-linker of actin filaments. The region containing immunoglobulin type modules 19-21 makes up the binding site for the cytoplasmic tails of the integrin adhesion receptors. Here we investigate the stability of the Ig-like filamin domains using NMR studies over a range of pH and temperature. We show that the 21st Ig-like module (FLNa21) is partly unfolded even under physiological conditions an...

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Authors: Jiang, P; Campbell, I

• Journal: Biochemistry
• Volume: 47
• Issue: 42
• Pages: 11055-11061
• Publication date: 2008-10-01
• DOI: 10.1021/bi8011466
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Humans; Protein Folding; Thermodynamics; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; Protein Conformation; Peptide Fragments; Integrins; Microfilament Proteins; Hydrogen-Ion Concentration; Binding Sites; Drug Stability; Immunoglobulins; Models, Molecular; Contractile Proteins