Ring and zipper formation is the key to understanding the structural variety in all-β proteins

Ryotaro Koike; Kengo Kinoshita; Akinori Kidera

doi:10.1016/S0014-5793(02)03729-8

Ring and zipper formation is the key to understanding the structural variety in all-β proteins

Ryotaro Koike, Kengo Kinoshita, Akinori Kidera

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

3 Citations (Scopus)

Abstract

A novel structural classification of β proteins is presented from the viewpoint of the ring-shaped structure and the zipper-like contact pattern, based on the fact that 92% and 60% of β proteins have the ring topology and the zippered contact pattern, respectively. We discuss the implication of the unexpectedly high preference for the ring and zippered structures in connection with the folding process of β proteins.

Original language	English
Pages (from-to)	9-13
Number of pages	5
Journal	FEBS Letters
Volume	533
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03729-8
Publication status	Published - 2003 Jan 2
Externally published	Yes

Keywords

Classification of β proteins
Protein three-dimensional structure
Relative contact order
Ring structure
Zippered structure

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(02)03729-8

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abstract = "A novel structural classification of β proteins is presented from the viewpoint of the ring-shaped structure and the zipper-like contact pattern, based on the fact that 92% and 60% of β proteins have the ring topology and the zippered contact pattern, respectively. We discuss the implication of the unexpectedly high preference for the ring and zippered structures in connection with the folding process of β proteins.",

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AU - Kinoshita, Kengo

AU - Kidera, Akinori

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KW - Classification of β proteins

KW - Protein three-dimensional structure

KW - Relative contact order

KW - Ring structure

KW - Zippered structure

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