2bx6

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models PDB ID 2bx6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.1Å
Sites:
Ligands:
Coordinates:	save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF THE HUMAN RETINITIS PIGMENTOSA PROTEIN 2 (RP2)

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: Retinitis pigmentosa-2 OMIM:[312600], Xp11.3 deletion syndrome OMIM:[312600]

About this Structure

2BX6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3., Kuhnel K, Veltel S, Schlichting I, Wittinghofer A, Structure. 2006 Feb;14(2):367-78. PMID:16472755

Page seeded by OCA on Thu Mar 20 16:07:53 2008