Lysophosphatidic acid and lipopolysaccharide bind to the PIP2-binding domain of gelsolin.
Biochim Biophys Acta
; 1758(1): 85-9, 2006 Jan.
Article
em En
| MEDLINE
| ID: mdl-16460666
ABSTRACT
The binding of the gelsolin P2 peptide (residues 150-169) with lysophosphatidic acid (LPA) and lipopolysaccharide (LPS) was investigated by isothermal titration calorimetry. P2 binds to LPS with higher affinity than to LPA. For the interaction of 1-oleoyl-LPA with P2 in the absence of salt, K(d) and deltaH degrees were 920 nM and -2.07 kcal/mol, respectively, at pH 7.4 and 25 degrees C. For the interaction of lipopolysaccharide (LPS) from P. aeruginosa with P2 under the same conditions, K(d) was 177 nM and deltaH degrees was -7.6 kcal/mol.
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Base de dados:
MEDLINE
Assunto principal:
Lisofosfolipídeos
/
Lipopolissacarídeos
/
Estrutura Terciária de Proteína
/
Gelsolina
/
Fosfatidilinositol 4,5-Difosfato
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Estados Unidos