PDB ID or protein name

1h0a » Epsin-1 (ENTH domain)

1h0a » Epsin-1 (ENTH domain)
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Topology in Eukaryotic plasma membrane
Topologyextracellular side
cytoplasmic side
1h0a » Epsin-1 (ENTH domain)
Depth 3.2 ± 1.1 Å
Tilt Angle 39 ± 19°
ΔGtransfer -5.3 kcal/mol
Links to 1h0a PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 1.70 Å
Other PDB entries representing this structure 1edu, 1eyh, 1inz
Number of subunits 1
Experimental Verification for 1h0a » Epsin-1 (ENTH domain)
N-terminal helix (residues L6 and M10) penetrates the hydrophobic core of lipid bilayers in the presence of inositol lipids (Stahelin et al. 2003), which is consistent with the calculated orientation (L6, M10, I13 and V14 are buried in the hydrophobic interior of the membrane). Maximal membrane binding affinity is -10.5 kcal/mol (Stahelin et al. 2003), which is higher than the calculated transfer energy due to specific binding of phosphoinositides.
1 reference
Stahelin RV, Long F, Peter BJ, Murray D, De Camilli P, McMahon HT, Cho W. Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. 2003 Aug 1;278(31):28993-9. PubMed
Comments on 1h0a » Epsin-1 (ENTH domain)
Binds to membranes enriched in phosphatidylinositol-4,5-biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis. Additional membrane-anchoring elements: inositol lipids that are specifically bound to the protein. N-terminal domain of epsin-4 (1xgw) was also identified as membrane-associated though its N-terminus in calculations.