Correlation between binding and dynamics at SH2 domain interfaces (Q57202409)

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9 November 2019

title

Correlation between binding and dynamics at SH2 domain interfaces (English)

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9 November 2019

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5

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9 November 2019

author name string

D R Muhandiram

2

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9 November 2019

L E Kay

1

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9 November 2019

G Wolf

3

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9 November 2019

S E Shoelson

4

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9 November 2019

publication date

1 February 1998

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Nature structural biology

9 November 2019

published in

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9 November 2019

volume

5

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9 November 2019

issue

2

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9 November 2019

page(s)

156-163

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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

9 November 2019

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Correlation between dynamics and high affinity binding in an SH2 domain interaction

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Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme

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13C NMR relaxation studies of backbone and side chain motion of the catalytic tyrosine residue in free and steroid-bound delta 5-3-ketosteroid isomerase

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SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

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SH2 domains recognize specific phosphopeptide sequences

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Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity

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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

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Effects of ion binding on the backbone dynamics of calbindin D9k determined by 15N NMR relaxation

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Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor. Deuterium NMR studies in solution and in the solid state

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31 March 2020

Identifiers

DOI

10.1038/NSB0298-156

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9461082%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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