2BX6

Crystal Structure of the human Retinitis Pigmentosa protein 2 (RP2)

2BX6 の概要

• エントリーDOI: 10.2210/pdb2bx6/pdb
• 分子名称: XRP2 PROTEIN, SULFATE ION (3 entities in total)
• 機能のキーワード: transduction protein, retinitis pigmentosa, sensory transduction, vision
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side: O75695
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39779.04

構造登録者

Kuhnel, K.,Veltel, S.,Schlichting, I.,Wittinghofer, A. (登録日: 2005-07-24, 公開日: 2006-01-18, 最終更新日: 2024-05-08)

主引用文献

Kuhnel, K.,Veltel, S.,Schlichting, I.,Wittinghofer, A.
Crystal Structure of the Human Retinitis Pigmentosa 2 Protein and its Interaction with Arl3
Structure, 14:367-, 2006

PubMed Abstract: The crystal structure of human retinitis pigmentosa 2 protein (RP2) was solved to 2.1 angstroms resolution. It consists of an N-terminal beta helix and a C-terminal ferredoxin-like alpha/beta domain. RP2 is functionally and structurally related to the tubulin-specific chaperone cofactor C. Seven of nine known RP2 missense mutations identified in patients are located in the beta helix domain, and most of them cluster to the hydrophobic core and are likely to destabilize the protein. Two residues, Glu138 and the catalytically important Arg118, are solvent-exposed and form a salt bridge, indicating that Glu138 might be critical for positioning Arg118 for catalysis. RP2 is a specific effector protein of Arl3. The N-terminal 34 residues and beta helix domain of RP2 are required for this interaction. The abilitities of RP2 to bind Arl3 and cause retinitis pigmentosa seem to be correlated, since both the R118H and E138G mutants show a drastically reduced affinity to Arl3.

PubMed: 16472755
DOI: 10.1016/J.STR.2005.11.008

実験手法

X-RAY DIFFRACTION (2.1 Å)