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

Kód výsledku v 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>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FD - Onkologie a hematologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2010

Kód důvěrnosti údajů

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

Název periodika

Journal of molecular biology

ISSN

0022-2836

e-ISSN

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Svazek periodika

404

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

21

Strana od-do

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Kód UT WoS článku

000285372700007

EID výsledku v databázi Scopus

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