The tandem β-zipper: modular binding of tandem domains and linear motifs.

Jennifer Robyn Potts; Jacqueline Matthews

doi:10.1016/j.febslet.2013.01.002

The tandem β-zipper: modular binding of tandem domains and linear motifs.

Jennifer Robyn Potts, Jacqueline Matthews

Biology

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

Abstract

The tandem β-zipper protein-protein binding interface involves an intrinsically disordered protein (IDP) binding two or more globular domains through β-sheet-augmentation in a modular fashion, and represents a paradigm in IDP-mediated protein-protein interactions. While characterised tandem β-zippers are rare, known examples are associated with diverse biological processes. A combination of their advantages (binding specificity and the ability to generate high affinity binding sites by linking multiple lower affinity motifs) and the prevalence of both tandem domains and IDPs points to the existence of many more β-zippers in nature. The characterisation of these interactions has greatly enhanced the understanding of the biological systems involved but given their apparent tolerance to mutation, detecting other tandem β-zipper interactions using bioinformatics may be challenging.

Original language	English
Pages (from-to)	1164-1171
Journal	FEBS Letters
Volume	587
Issue number	8
DOIs	https://doi.org/10.1016/j.febslet.2013.01.002
Publication status	Published - 17 Apr 2013

Access to Document

10.1016/j.febslet.2013.01.002

http://www.sciencedirect.com/science/article/pii/S0014579313000161

Cite this

@article{6c3207b54640425b8d80c0cbce3d1586,

title = "The tandem β-zipper: modular binding of tandem domains and linear motifs.",

abstract = "The tandem β-zipper protein-protein binding interface involves an intrinsically disordered protein (IDP) binding two or more globular domains through β-sheet-augmentation in a modular fashion, and represents a paradigm in IDP-mediated protein-protein interactions. While characterised tandem β-zippers are rare, known examples are associated with diverse biological processes. A combination of their advantages (binding specificity and the ability to generate high affinity binding sites by linking multiple lower affinity motifs) and the prevalence of both tandem domains and IDPs points to the existence of many more β-zippers in nature. The characterisation of these interactions has greatly enhanced the understanding of the biological systems involved but given their apparent tolerance to mutation, detecting other tandem β-zipper interactions using bioinformatics may be challenging.",

author = "Potts, {Jennifer Robyn} and Jacqueline Matthews",

year = "2013",

month = apr,

day = "17",

doi = "10.1016/j.febslet.2013.01.002",

language = "English",

volume = "587",

pages = "1164--1171",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley-Blackwell",

number = "8",

}

TY - JOUR

T1 - The tandem β-zipper

T2 - modular binding of tandem domains and linear motifs.

AU - Potts, Jennifer Robyn

AU - Matthews, Jacqueline

PY - 2013/4/17

Y1 - 2013/4/17

N2 - The tandem β-zipper protein-protein binding interface involves an intrinsically disordered protein (IDP) binding two or more globular domains through β-sheet-augmentation in a modular fashion, and represents a paradigm in IDP-mediated protein-protein interactions. While characterised tandem β-zippers are rare, known examples are associated with diverse biological processes. A combination of their advantages (binding specificity and the ability to generate high affinity binding sites by linking multiple lower affinity motifs) and the prevalence of both tandem domains and IDPs points to the existence of many more β-zippers in nature. The characterisation of these interactions has greatly enhanced the understanding of the biological systems involved but given their apparent tolerance to mutation, detecting other tandem β-zipper interactions using bioinformatics may be challenging.

AB - The tandem β-zipper protein-protein binding interface involves an intrinsically disordered protein (IDP) binding two or more globular domains through β-sheet-augmentation in a modular fashion, and represents a paradigm in IDP-mediated protein-protein interactions. While characterised tandem β-zippers are rare, known examples are associated with diverse biological processes. A combination of their advantages (binding specificity and the ability to generate high affinity binding sites by linking multiple lower affinity motifs) and the prevalence of both tandem domains and IDPs points to the existence of many more β-zippers in nature. The characterisation of these interactions has greatly enhanced the understanding of the biological systems involved but given their apparent tolerance to mutation, detecting other tandem β-zipper interactions using bioinformatics may be challenging.

U2 - 10.1016/j.febslet.2013.01.002

DO - 10.1016/j.febslet.2013.01.002

M3 - Article

SN - 0014-5793

VL - 587

SP - 1164

EP - 1171

JO - FEBS Letters

JF - FEBS Letters

IS - 8

ER -