2bx6
From Proteopedia
| Line 6: | Line 6: | ||
==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=312600 312600]], Xp11.3 deletion syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=312600 312600]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 23: | Line 26: | ||
[[Category: vision]] | [[Category: vision]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:07:08 2007'' |
Revision as of 19:00, 12 November 2007
|
CRYSTAL STRUCTURE OF THE HUMAN RETINITIS PIGMENTOSA PROTEIN 2 (RP2)
Contents |
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 with SO4 as ligand. Structure known Active Site: AC1. 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 Mon Nov 12 21:07:08 2007
