GPR180 is a new member of the Golgi-dynamics domain seven-transmembrane helix protein family
Sarah-Ana Mitrovic, Chamalee Demalgiriya-Gamage, Lisa-Maria Winter, Tobias Kiechle, Rebecca Ebenhoch, Heike Neubauer, Birgit Stierstorfer, Lee Frego, Christian Wolfrum, Sophia Reindl, Herbert Nar · 2024
Read GPR180 is a new member of the Golgi-dynamics domain seven-transmembrane helix protein family by Sarah-Ana Mitrovic, Chamalee Demalgiriya-Gamage, Lisa-Maria Winter, Tobias Kiechle, Rebecca Ebenhoch, Heike Neubauer, Birgit Stierstorfer, Lee Frego, Christian Wolfrum, Sophia Reindl, Herbert Nar (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11605061.txt.
Description
Sarah-Ana Mitrovic and co-authors study a cell protein called GPR180 in a 2024 paper. The protein may join a family of proteins that move cargo across cell membranes. Family members share a front part named the GOLD domain, which may sense binding partners.
The team solved the shape of the front part of GPR180 and confirmed the match to GOLD domains. Images show the protein sits in small inner cell sacs that face acid conditions. Tests found shape changes that depend on acid level, mapped to a likely binding site. The work gives a first clear view of what this protein does inside cells.
Catalog record
| CREATOR | Sarah-Ana Mitrovic, Chamalee Demalgiriya-Gamage, Lisa-Maria Winter, Tobias Kiechle, Rebecca Ebenhoch, Heike Neubauer, Birgit Stierstorfer, Lee Frego, Christian Wolfrum, Sophia Reindl, Herbert Nar |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 65 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |