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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, Vol. 14, No. 2, 01.02.2006, p. 367-78.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kühnel, K, Veltel, S, Schlichting, I & Wittinghofer, A 2006, 'Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3', STRUCTURE, vol. 14, no. 2, pp. 367-78. https://doi.org/10.1016/j.str.2005.11.008

APA

Kühnel, K., Veltel, S., Schlichting, I., & Wittinghofer, A. (2006). Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. STRUCTURE, 14(2), 367-78. https://doi.org/10.1016/j.str.2005.11.008

Vancouver

Kühnel K, Veltel S, Schlichting I, Wittinghofer A. Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. STRUCTURE. 2006 Feb 1;14(2):367-78. https://doi.org/10.1016/j.str.2005.11.008

Bibtex

@article{6a45bff0cb5b4f8da98c8e9f716a85dd,
title = "Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3",
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.",
keywords = "ADP-Ribosylation Factors, Amino Acid Sequence, Animals, Arginine, Binding Sites, Catalysis, Crystallography, X-Ray, Eye Proteins, Ferredoxins, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Missense, Protein Structure, Secondary, Protein Structure, Tertiary, Retinitis Pigmentosa, Sequence Alignment",
author = "Karin K{\"u}hnel and Stefan Veltel and Ilme Schlichting and Alfred Wittinghofer",
year = "2006",
month = feb,
day = "1",
doi = "10.1016/j.str.2005.11.008",
language = "English",
volume = "14",
pages = "367--78",
journal = "STRUCTURE",
issn = "0969-2126",
publisher = "Cell Press",
number = "2",

}

RIS

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 -