Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10297299" target="_blank" >RIV/00216208:11310/15:10297299 - isvavai.cz</a>

Alternative codes found

RIV/68378050:_____/15:00458058 RIV/61388963:_____/15:00454556

Result on the web

<a href="http://www.nature.com/ncomms/2015/150806/ncomms8968/full/ncomms8968.html" target="_blank" >http://www.nature.com/ncomms/2015/150806/ncomms8968/full/ncomms8968.html</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/ncomms8968" target="_blank" >10.1038/ncomms8968</a>

Result language

angličtina

Original language name

Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif

Original language description

Lens epithelium-derived growth factor (LEDGF/p75) is an epigenetic reader and attractive therapeutic target involved in HIV integration and the development of mixed lineage leukaemia (MLL1) fusion-driven leukaemia. Besides HIV integrase and the MLL1-menin complex, LEDGF/p75 interacts with various cellular proteins via its integrase binding domain (IBD). Here we present structural characterization of IBD interactions with transcriptional repressor JPO2 and domesticated transposase PogZ, and show that thePogZ interaction is nearly identical to the interaction of LEDGF/p75 with MLL1. The interaction with the IBD is maintained by an intrinsically disordered IBD-binding motif (IBM) common to all known cellular partners of LEDGF/p75. In addition, based on IBM conservation, we identify and validate IWS1 as a novel LEDGF/p75 interaction partner. Our results also reveal how HIV integrase efficiently displaces cellular binding partners from LEDGF/p75. Finally, the similar binding modes of LEDGF

Czech name

—

Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Nature Communications

ISSN

2041-1723

e-ISSN

—

Volume of the periodical

6

Issue of the periodical within the volume

AUG 2015

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

1-14

UT code for WoS article

000360346900009

EID of the result in the Scopus database

2-s2.0-84938863492