| Structural highlights
4znq is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.9Å |
| Ligands: | CL, EDO, EPE, MAN, PEG, PG4, PGE, PRD_900111 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AEP1_DANRE Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycans, and also requires a low pH environment. In vitro, shows high binding affinity for S.cerevisiae mannan and human HIV virus glycoprotein gp120.[1]
References
- ↑ Jia N, Liu N, Cheng W, Jiang YL, Sun H, Chen LL, Peng J, Zhang Y, Ding YH, Zhang ZH, Wang X, Cai G, Wang J, Dong MQ, Zhang Z, Wu H, Wang HW, Chen Y, Zhou CZ. Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein. EMBO Rep. 2015 Dec 28. pii: e201540851. PMID:26711430 doi:https://dx.doi.org/10.15252/embr.201540851
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