A Divergent substrate-binding loop within the pro-oncogenic protein anterior gradient-2 forms a docking site for Reptin

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F10%3A%230000121" target="_blank" >RIV/00209805:_____/10:#0000121 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

A Divergent substrate-binding loop within the pro-oncogenic protein anterior gradient-2 forms a docking site for Reptin

Original language description

Anterior gradient-2 (AGR2) functions in a range of biological systems, however there are no well-validated binding proteins for AGR2 protein. The yeast two-hybrid system was used to isolate the ATP binding protein Reptin as an AGR2-interacting protein. AGR2 formed a stable complex in human cell lysates with Reptin. To evaluate the effects of ATP on Reptin?AGR2 complex stability, mutations were made at the two ATP binding motifs in Reptin reasulting in mutants with altered oligomerization, thermostability, and AGR2 binding properties. ATP binding motifs of Reptin thus play a role in regulating the stability of the AGR2?Reptin complex. The Reptin docking site was mapped to a divergent octapeptide loop in the AGR2 superfamily between amino acids 104 and 111. Mutations at codon Y104 or F111 in full-length AGR2 destabilized the binding of Reptin. These data highlight the existence of a protein docking motif on AGR2 and an ATP-regulated peptide-binding activity for Reptin.

Czech name

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Czech description

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Type

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

CEP classification

FD - Oncology and haematology

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

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2010

Confidentiality

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

Name of the periodical

Journal of molecular biology

ISSN

0022-2836

e-ISSN

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Volume of the periodical

404

Issue of the periodical within the volume

3

Country of publishing house

GB - UNITED KINGDOM

Number of pages

21

Pages from-to

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UT code for WoS article

000285372700007

EID of the result in the Scopus database

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