Back to search

Article

Deep mutational scanning of a multi-domain signaling protein reveals mechanisms of regulation and pathogenicity

2024-05-13

Abstract excerpt

Multi-domain signaling enzymes are often regulated through extensive inter-domain interactions, and disruption of inter-domain interfaces by mutations can lead to aberrant signaling and diseases. For example, the tyrosine phosphatase SHP2 contains two phosphotyrosine recognition domains that auto-inhibit its catalytic domain. SHP2 is canonically activated by binding of these non-catalytic domains to phosphoprotein...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
c7122ce0-ae72-5e98-ab8f-085dd813bc7d
DOI
10.1101/2024.05.13.593907
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Deep mutational scanning of a multi-domain signaling protein reveals mechanisms of regulation and pathogenicityDOI 10.1101/2024.05.13.593907
Select a neighboring publication to make it the new centre.