2EMT

Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1

2EMT の概要

• エントリーDOI: 10.2210/pdb2emt/pdb
• 関連するPDBエントリー: 1GC6 1GC7 1J19 2D10 2D11 2D2Q 2EMS
• 分子名称: Radixin, P-selectin glycoprotein ligand 1 (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 (house mouse); 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043; Cell membrane ; Single-pass membrane protein : Q62170
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 82633.00

構造登録者

Takai, Y.,Kitano, K.,Terawaki, S.,Maesaki, R.,Hakoshima, T. (登録日: 2007-03-28, 公開日: 2008-03-18, 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 PSGL-1 binding to ERM proteins
Genes Cells, 12:1329-1338, 2007

PubMed Abstract: P-selectin glycoprotein ligand-1 (PSGL-1), an adhesion molecule with O-glycosylated extracellular sialomucins, is involved in leukocyte inflammatory responses. On activation, ezrin-radixin-moesin (ERM) proteins mediate the redistribution of PSGL-1 on polarized cell surfaces to facilitate binding to target molecules. ERM proteins recognize a short binding motif, Motif-1, conserved in cytoplasmic tails of adhesion molecules, whereas PSGL-1 lacks Motif-1 residues important for binding to ERM proteins. The crystal structure of the complex between the radixin FERM domain and a PSGL-1 juxtamembrane peptide reveals that the peptide binds the groove of FERM subdomain C by forming a beta-strand associated with strand beta5C, followed by a loop flipped out towards the solvent. The Motif-1 3(10) helix present in the FERM-ICAM-2 complex is absent in PSGL-1 given the absence of a critical Motif-1 alanine residue, and PSGL-1 reduces its contact area with subdomain C. Non-conserved positions are occupied by large residues Met9 and His8, which stabilize peptide conformation and enhance groove binding. Non-conserved residues play an important role in compensating for loss of binding energy resulting from the absence of conserved residues important for binding.

PubMed: 18076570
DOI: 10.1111/j.1365-2443.2007.01137.x

実験手法

X-RAY DIFFRACTION (2.8 Å)