Proteins with leucine-rich repeats

Bostjan Kobe; Johann Deisenhofer

doi:10.1016/0959-440X(95)80105-7

Proteins with leucine-rich repeats

Bostjan Kobe, Johann Deisenhofer

Research output: Contribution to journal › Article › peer-review

327 Scopus citations

Abstract

Luecine-rich repeats are short sequence motifs present in over sixty proteins, all of which appear to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor demonstrated that the repeats correspond to β-α structural units. The recently determined crystal structure of the ribonuclease A-ribonuclease inhibitor complex suggests the basis for the protein-binding function of leucine-rich repeats.

Original language	English (US)
Pages (from-to)	409-416
Number of pages	8
Journal	Current Opinion in Structural Biology
Volume	5
Issue number	3
DOIs	https://doi.org/10.1016/0959-440X(95)80105-7
State	Published - Jun 1995

Keywords

LPS-lipopolysaccharide
LRR-leucine-rich repeat
RI-ribonuclease inhibitor

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/0959-440X(95)80105-7

Cite this

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title = "Proteins with leucine-rich repeats",

abstract = "Luecine-rich repeats are short sequence motifs present in over sixty proteins, all of which appear to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor demonstrated that the repeats correspond to β-α structural units. The recently determined crystal structure of the ribonuclease A-ribonuclease inhibitor complex suggests the basis for the protein-binding function of leucine-rich repeats.",

keywords = "LPS-lipopolysaccharide, LRR-leucine-rich repeat, RI-ribonuclease inhibitor",

author = "Bostjan Kobe and Johann Deisenhofer",

year = "1995",

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T1 - Proteins with leucine-rich repeats

AU - Kobe, Bostjan

AU - Deisenhofer, Johann

PY - 1995/6

Y1 - 1995/6

N2 - Luecine-rich repeats are short sequence motifs present in over sixty proteins, all of which appear to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor demonstrated that the repeats correspond to β-α structural units. The recently determined crystal structure of the ribonuclease A-ribonuclease inhibitor complex suggests the basis for the protein-binding function of leucine-rich repeats.

AB - Luecine-rich repeats are short sequence motifs present in over sixty proteins, all of which appear to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor demonstrated that the repeats correspond to β-α structural units. The recently determined crystal structure of the ribonuclease A-ribonuclease inhibitor complex suggests the basis for the protein-binding function of leucine-rich repeats.

KW - LPS-lipopolysaccharide

KW - LRR-leucine-rich repeat

KW - RI-ribonuclease inhibitor

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U2 - 10.1016/0959-440X(95)80105-7

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JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 3

ER -

Proteins with leucine-rich repeats

Abstract

Keywords

ASJC Scopus subject areas

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