2ems
From Proteopedia
Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43
Overview
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.
About this Structure
2EMS is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):49-51. Epub 2006 Dec 22. PMID:17183174 Page seeded by OCA on Sun May 4 02:48:09 2008
