Cargando…
Mutational analysis of human profilin I reveals a second PI(4,5)-P(2) binding site neighbouring the poly(L-proline) binding site
BACKGROUND: Profilin is a small cytoskeletal protein which interacts with actin, proline-rich proteins and phosphatidylinositol 4,5-bisphosphate (PI(4,5)-P(2)). Crystallography, NMR and mutagenesis of vertebrate profilins have revealed the amino acid residues that are responsible for the interaction...
Autores principales: | Lambrechts, Anja, Jonckheere, Veronique, Dewitte, Daisy, Vandekerckhove, Joel, Ampe, Christophe |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2002
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC116585/ https://www.ncbi.nlm.nih.gov/pubmed/12052260 http://dx.doi.org/10.1186/1471-2091-3-12 |
Ejemplares similares
-
Structure of the second phosphoubiquitin–binding site in parkin
por: Fakih, Rayan, et al.
Publicado: (2022) -
Function of interfacial prolines at the transmitter-binding sites of the neuromuscular acetylcholine receptor.
por: Gupta, Shaweta, et al.
Publicado: (2013) -
Computational predictions of common transcription factor binding sites on the genes of proline metabolism in plants
por: Kiran, Usha, et al.
Publicado: (2012) -
Identification and expression analysis of splice variants of mouse enabled homologue during development and in adult tissues
por: Veniere, Sylvie, et al.
Publicado: (2010) -
Reversible binding of actin to gelsolin and profilin in human platelet extracts
Publicado: (1987)