3RRC

Crystal Structure of Region II from Plasmodium vivax Duffy Binding Protein

3RRC の概要

• エントリーDOI: 10.2210/pdb3rrc/pdb
• 分子名称: Duffy receptor, 1,2-ETHANEDIOL, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: duffy binding like, receptor recognition, duffy antigen receptor for chemokines, cell invasion
• 由来する生物種: Plasmodium vivax
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P22290
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76342.92

構造登録者

Tolia, N.H. (登録日: 2011-04-29, 公開日: 2011-07-13, 最終更新日: 2024-11-27)

主引用文献

Batchelor, J.D.,Zahm, J.A.,Tolia, N.H.
Dimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARC.
Nat.Struct.Mol.Biol., 18:908-914, 2011

PubMed Abstract: Plasmodium vivax and Plasmodium knowlesi invasion depends on the parasite Duffy-binding protein DBL domain (RII-PvDBP or RII-PkDBP) engaging the Duffy antigen receptor for chemokines (DARC) on red blood cells. Inhibition of this key interaction provides an excellent opportunity for parasite control. There are competing models for whether Plasmodium ligands engage receptors as monomers or dimers, a question whose resolution has profound implications for parasite biology and control. We report crystallographic, solution and functional studies of RII-PvDBP showing that dimerization is required for and driven by receptor engagement. This work provides a unifying framework for prior studies and accounts for the action of naturally acquired blocking antibodies and the mechanism of immune evasion. We show that dimerization is conserved in DBL-domain receptor engagement and propose that receptor-mediated ligand dimerization drives receptor affinity and specificity. Because dimerization is prevalent in signaling, our studies raise the possibility that induced dimerization may activate pathways for invasion.

PubMed: 21743458
DOI: 10.1038/nsmb.2088

実験手法

X-RAY DIFFRACTION (1.95 Å)