Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3
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Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. / Kühnel, Karin; Veltel, Stefan; Schlichting, Ilme; Wittinghofer, Alfred.
in: STRUCTURE, Jahrgang 14, Nr. 2, 01.02.2006, S. 367-78.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3
AU - Kühnel, Karin
AU - Veltel, Stefan
AU - Schlichting, Ilme
AU - Wittinghofer, Alfred
PY - 2006/2/1
Y1 - 2006/2/1
N2 - 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.
AB - 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.
KW - ADP-Ribosylation Factors
KW - Amino Acid Sequence
KW - Animals
KW - Arginine
KW - Binding Sites
KW - Catalysis
KW - Crystallography, X-Ray
KW - Eye Proteins
KW - Ferredoxins
KW - Humans
KW - Intracellular Signaling Peptides and Proteins
KW - Membrane Proteins
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Mutation, Missense
KW - Protein Structure, Secondary
KW - Protein Structure, Tertiary
KW - Retinitis Pigmentosa
KW - Sequence Alignment
U2 - 10.1016/j.str.2005.11.008
DO - 10.1016/j.str.2005.11.008
M3 - SCORING: Journal article
C2 - 16472755
VL - 14
SP - 367
EP - 378
JO - STRUCTURE
JF - STRUCTURE
SN - 0969-2126
IS - 2
ER -