2EMS

Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule CD43

2EMS の概要

• エントリーDOI: 10.2210/pdb2ems/pdb
• 関連するPDBエントリー: 2EMT
• 分子名称: Radixin, Leukosialin (2 entities in total)
• 機能のキーワード: protein-peptide complex, cell adhesion
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043; Membrane; Single-pass type I membrane protein: P15702
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40203.24

構造登録者

Takai, Y.,Kitano, K.,Terawaki, S.,Maesaki, R.,Hakoshima, T. (登録日: 2007-03-28, 公開日: 2008-04-01, 最終更新日: 2023-10-25)

主引用文献

Takai, Y.,Kitano, K.,Terawaki, S.,Maesaki, R.,Hakoshima, T.
Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins
J.Mol.Biol., 381:634-644, 2008

PubMed Abstract: CD43/leukosialin/sialophorin is the major adhesion molecule in most hematopoietic cells and belongs to the sialomucin superfamily. In leukocyte emigration and activation, the exclusion of CD43 from the immunological synapse is an essential step. While the exclusion requires binding of the cytoplasmic region to ERM (ezrin/radixin/moesin) proteins, the detailed specific nature of the interaction between CD43 and ERM proteins is obscure. We have characterized the conformational properties of the CD43 cytoplasmic region, consisting of 124 amino acid residues, by hydrodynamic and spectroscopic measurements. Sedimentation equilibrium and velocity studies of ultracentrifugation revealed that the CD43 cytoplasmic peptide exists in a monomeric and extended form in solution. The crystal structure of the complex between the radixin FERM (4.1 and ERM) domain and the CD43 juxtamembrane region peptide reveals that the nonpolar region of the peptide binds subdomain C of the FERM domain. CD43 lacks the Motif-1 sequence for FERM binding found in the FERM-intercellular adhesion molecule-2 complex but possesses two conserved leucine residues that dock into the hydrophobic pocket of subdomain C without forming a 3(10)-helix. The FERM-binding site on CD43 is overlapped with the functional nuclear localization signal sequence. Our structure suggests that regulation of ERM binding may be coupled with regulated intramembrane proteolysis of CD43 followed by the nuclear transfer of the cytoplasmic peptide.

PubMed: 18614175
DOI: 10.1016/j.jmb.2008.05.085

実験手法

X-RAY DIFFRACTION (2.9 Å)