Stannin

Stannins are small proteins that consist of a single transmembrane helix, an unstructured linker domain, and a cytoplasmic domain. The transmembrane region contains a conserved cysteine residue (Cys32) that, together with Cys34 found in the stannin unstructured linker domain, constitutes the putative trimethyltin-binding site, close to the lipid/solvent interface.[1]

Stannin
Identifiers
Symbol	SNN_transmemb
Pfam	PF09049
InterPro	IPR015135
OPM superfamily	47
OPM protein	1zza
Membranome	104
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

The unstructured protein region connects two adjacent helical domains. It contains a conserved CXC metal-binding motif and a putative 14-3-3-zeta binding domain. Upon coordinating dimethytin, considerable structural or dynamic changes in the flexible loop region of SNN may take place, recruiting other binding partners such as 14-3-3-zeta, and thereby initiating the apoptotic cascade.[1]

The cytoplasmic domain forms a distorted helix that is partially absorbed into the plane of the lipid bilayer. It interacts with the surface of the lipid bilayer, and contributes to the initiation of the apoptotic cascade on binding of the unstructured linker domain to dimethyltin.[1]

Human proteins containing this domain

SNN;

References

1. Mascioni A, Veglia G, Buck-Koehntop BA, Buffy JJ (2005). "Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride". J. Mol. Biol. 354 (3): 652–65. doi:10.1016/j.jmb.2005.09.038. PMID 16246365.

This article incorporates text from the public domain Pfam and InterPro: IPR015136