ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 7 citations in OpenAlex.
- Structural Basis for the Interaction between the Ezrin FERM-Domain and Human Aquaporins.International journal of molecular sciences · 2024Article
- Article
- Targeting GABAFrontiers in molecular neuroscience · 2019Article
- Radixin inhibition decreases adult neural progenitor cell migration and proliferation in vitro and in vivo.Frontiers in cellular neuroscience · 2013Article
- Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Radixin is a member of the ERM proteins that cross-link plasma membranes and actin filaments. The FERM domains located in the N-terminal regions of ERM proteins are responsible for membrane association through direct interaction with the cytoplasmic tails of integral membrane proteins. Here, crystals of the radixin FERM domain bound to the cytoplasmic peptides of two adhesion molecules, CD43 and PSGL-1, have been obtained. Crystals of the radixin FERM domain bound to CD43 belong to space group P4(3)22, with unit-cell parameters a = b = 68.72, c = 201.39 A, and contain one complex in the crystallographic asymmetric unit. Crystals of the radixin FERM domain bound to PSGL-1 belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 A, and contain two complexes in the crystallographic asymmetric unit. Intensity data sets were collected to a resolution of 2.9 A for the FERM-CD43 complex and 2.8 A for the FERM-PSGL-1 complex.
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