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Journal article

An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering

Abstract:

Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function. Here, we have identified allosteric sites in protein tyrosine phosphatase 1B (PTP1B) by combining multiple-temperature X-ray crystallography experiments and structure determination from hundreds of individual small- molecule fragment soaks. New mo...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.7554/eLife.36307.001

Authors


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Helen Hay Whitney Foundation More from this funder
A.P. Giannini Foundation More from this funder
Wellcome Trust More from this funder
David and Lucile Packard Foundation More from this funder
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Publisher:
eLife Sciences Publications Publisher's website
Journal:
eLife Journal website
Volume:
7
Pages:
e36307
Publication date:
2018-06-07
Acceptance date:
2018-06-04
DOI:
EISSN:
2050-084X
ISSN:
2050-084X
Source identifiers:
891906
Pubs id:
pubs:891906
UUID:
uuid:883b9c80-6cf1-414d-b385-27cec47e38c8
Local pid:
pubs:891906
Deposit date:
2018-08-02

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