WW and SH3 domains, two different scaffolds to recognize proline-rich ligands (Q28209648)

The WW domain: a signalling site in dystrophin?

Europe PubMed Central

title

WW and SH3 domains, two different scaffolds to recognize proline-rich ligands (English)

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Maria J Macias

1

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Silke Wiesner

object named as

Silke Wiesner

series ordinal

2

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author name string

Marius Sudol

series ordinal

3

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language of work or name

English

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publication date

20 February 2002

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published in

FEBS Letters

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volume

513

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issue

1

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page(s)

30-7

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cites work

1 reference

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NeW wrinkles for an old domain

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Structural analysis of WW domains and design of a WW prototype

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Structural basis for phosphoserine-proline recognition by group IV WW domains

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Solution structure of a Nedd4 WW domain-ENaC peptide complex

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Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan

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Solution structures of the YAP65 WW domain and the variant L30 K in complex with the peptides GTPPPPYTVG, N-(n-octyl)-GPPPY and PLPPY and the application of peptide libraries reveal a minimal binding epitope

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Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II.

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The WW Domain of Neural Protein FE65 Interacts with Proline-rich Motifs in Mena, the Mammalian Homolog of DrosophilaEnabled

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Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains

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10.1016/S0014-5793(01)03290-2

7 January 2021

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11911877

1 reference

Consolidated OpenCitations Corpus – April 2017