| BAR domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of amphiphysin BAR.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | BAR | ||||||||
| Pfam | PF03114 | ||||||||
| InterPro | IPR004148 | ||||||||
| SMART | SM00721 | ||||||||
| PROSITE | PDOC51021 | ||||||||
| SCOP2 | 1uru / SCOPe / SUPFAM | ||||||||
| CDD | cd07307 | ||||||||
| |||||||||
| Bin/amphiphysin/Rvs domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BAR-2 | ||||||||
| Pfam | PF10455 | ||||||||
| |||||||||
| BAR domain of APPL family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BAR-3 | ||||||||
| Pfam | PF16746 | ||||||||
| |||||||||
| EFC/F-BAR homology domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | FCH | ||||||||
| Pfam | PF00611 | ||||||||
| |||||||||
| Vps5 C terminal like (BAR domain) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Vps5 | ||||||||
| Pfam | PF09325 | ||||||||
| InterPro | IPR015404 | ||||||||
| |||||||||
| WASP-binding domain of sorting nexin proteins | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BAR-3-WASP | ||||||||
| Pfam | PF10456 | ||||||||
| |||||||||
In molecular biology, BAR domains are highly conserved protein dimerisation domains that occur in many proteins involved in membrane dynamics in a cell. The BAR domain is banana-shaped and binds to membrane via its concave face. It is capable of sensing membrane curvature by binding preferentially to curved membranes. BAR domains are named after three proteins that they are found in: Bin, Amphiphysin and Rvs.
- ^ Peter BJ, Kent HM, Mills IG, et al. (January 2004). "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure". Science. 303 (5657): 495–9. doi:10.1126/science.1092586. PMID 14645856. S2CID 6104655.