CASH--a beta-helix domain widespread among carbohydrate-binding proteins

F. D. Ciccarelli; R. R. Copley; T. Doerks; R. B. Russell; P. Bork

doi:10.1016/S0968-0004(01)02046-1

CASH--a beta-helix domain widespread among carbohydrate-binding proteins

F. D. Ciccarelli, R. R. Copley, T. Doerks, R. B. Russell, P. Bork

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

26 Citations (Scopus)

Abstract

In this article, we describe a novel, widespread domain (CASH) that is shared by many carbohydrate-binding proteins and sugar hydrolases. This domain occurs in more than 1000 proteins distributed among all three kingdoms of life. The CASH domain is characterized by internal repetitions of glycines and hydrophobic residues that correspond to the repetitive units of a predicted or observed right-handed beta-helix structure of the pectate lyase superfamily.

Original language	Undefined/Unknown
Article number	N/A
Pages (from-to)	59-62
Number of pages	4
Journal	TRENDS IN BIOCHEMICAL SCIENCES
Volume	27
Issue number	2
DOIs	https://doi.org/10.1016/S0968-0004(01)02046-1
Publication status	Published - 1 Feb 2002

Keywords

Ciccarelli

Access to Document

10.1016/S0968-0004(01)02046-1

Cite this

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abstract = "In this article, we describe a novel, widespread domain (CASH) that is shared by many carbohydrate-binding proteins and sugar hydrolases. This domain occurs in more than 1000 proteins distributed among all three kingdoms of life. The CASH domain is characterized by internal repetitions of glycines and hydrophobic residues that correspond to the repetitive units of a predicted or observed right-handed beta-helix structure of the pectate lyase superfamily.",

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AU - Copley, R. R.

AU - Doerks, T.

AU - Russell, R. B.

AU - Bork, P.

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AB - In this article, we describe a novel, widespread domain (CASH) that is shared by many carbohydrate-binding proteins and sugar hydrolases. This domain occurs in more than 1000 proteins distributed among all three kingdoms of life. The CASH domain is characterized by internal repetitions of glycines and hydrophobic residues that correspond to the repetitive units of a predicted or observed right-handed beta-helix structure of the pectate lyase superfamily.

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