Journal
BIOPHYSICAL JOURNAL
Volume 110, Issue 11, Pages 2463-2474Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2016.05.003
Keywords
-
Categories
Funding
- Deutsche Forschungsgemeinschaft [LA1272/6-1]
Ask authors/readers for more resources
Tetraspanins are master organizers in the plasma membrane, forming tetraspanin-enriched microdomains with one another and other surface molecules. Their rod-shaped structure includes a large extracellular loop (LEL) that plays a pivotal role in tetraspanin network formation. We performed comparative atomistic and coarse-grain molecular-dynamics simulations of the LEL in isolation and full-length CD81, and reproduced LEL flexibility patterns known from wet-lab experiments in which the LEL delta-loop region showed a pronounced flexibility. In a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine lipid bilayer and a plasma membrane environment, the conformational flexibility of the d-loop initiates CD81-CD81 contacts for oligomerization. Furthermore, in the plasma membrane, CD81-ganglioside bridges arising from preformed glycolipid patches cross-link the complexes. The data suggest that exposing a flexible domain enables binding to interaction partners by circumventing the restriction of orientation and conformational freedom of membrane proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available