Cargando…
Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain
Kindlins co-activate integrins alongside talin. They possess, like talin, a FERM domain (4.1-erythrin–radixin–moiesin domain) comprising F0–F3 subdomains, but with a pleckstrin homology (PH) domain inserted in the F2 subdomain that enables membrane association. We present the crystal structure of mu...
Autores principales: | Ni, Tao, Kalli, Antreas C., Naughton, Fiona B., Yates, Luke A., Naneh, Omar, Kozorog, Mirijam, Anderluh, Gregor, Sansom, Mark S.P., Gilbert, Robert J.C. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5290484/ https://www.ncbi.nlm.nih.gov/pubmed/27974389 http://dx.doi.org/10.1042/BCJ20160791 |
Ejemplares similares
-
Structural and Functional Characterization of the Kindlin-1 Pleckstrin Homology Domain
por: Yates, Luke A., et al.
Publicado: (2012) -
Interactions of Pleckstrin Homology Domains with Membranes: Adding Back the Bilayer via High-Throughput Molecular Dynamics
por: Yamamoto, Eiji, et al.
Publicado: (2016) -
Surface plasmon resonance and microscale thermophoresis approaches for determining the affinity of perforin for calcium ions
por: Naneh, Omar, et al.
Publicado: (2023) -
Systematic simulation of the interactions of pleckstrin homology domains with membranes
por: Le Huray, Kyle I. P., et al.
Publicado: (2022) -
Biophysical and Computational Studies of Membrane Penetration by the GRP1 Pleckstrin Homology Domain
por: Lumb, Craig N., et al.
Publicado: (2011)