- Source: ANTH domain
The ANTH domain is a membrane binding domain that shows weak specificity for PtdIns(4,5)P2. It was found in AP180 (homologous to CALM) endocytotic accessory protein that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.
Its structure is a solenoid of 9 helices. The PtdIns(4,5)P2 binding residues are spread over several helices at the tip of the structure. The PtdIns(4,5)P2 binding sequence is Kx9Kx(K/R)(H/Y).
An ANTH domain is also found in HIP1 and HIP1R, and the PtdIns(4,5)P2 binding sequence is conserved.
Human proteins containing this domain
HIP1; HIP1R; PICALM; SNAP91;
References
Further reading
Ford MG, Pearse BM, Higgins MK, et al. (February 2001). "Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes". Science. 291 (5506): 1051–5. CiteSeerX 10.1.1.407.6006. doi:10.1126/science.291.5506.1051. PMID 11161218.
External links
UMich Orientation of Proteins in Membranes protein/pdbid-1hfa - Calculated spatial position of ANTH domain of CALM protein in membrane
Kata Kunci Pencarian:
7.589
7.168
6.8
5.5
4
7.165
7.138
7.33
6.8
7.205
No More Posts Available.
No more pages to load.
