- Protein Classification
- Protein Links
 | lumenal side |
| cytoplasmic side |
| 1hyi » Early endosome antigen 1 (EEA1), monomer | |
|---|---|
| Depth | 3.0 ± 2.0 Å |
| Tilt Angle | 24 ± 17° |
| ΔGtransfer | -3.5 kcal/mol |
| Links to 1hyi | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | cytoplasmic |
| Resolution | NMR |
| Other PDB entries of this protein | 1hyj, 1joc |
| Number of subunits | 1 |
| Experimental Verification for 1hyi » Early endosome antigen 1 (EEA1), monomer |
|---|
| This orientation is in agreement with studies of monomeric FYVE domain in micelles, which shows that exposed V21 and T22 residues are buried in the hydrophobic core (Kutateladze and Overduin 2001, Brunecky et al. 2005). However, the orientations of monomeric FYVE domains change when they form a dimer through an additional coiled-coil domain (see 1joc). |
| 3 references |
|---|
| Brunecky R, Lee S, Rzepecki PW, Overduin M, Prestwich GD, Kutateladze AG, Kutateladze TG. 2005. Investigation of the binding geometry of a peripheral membrane protein. Biochemistry. 2005 44:16064-71. PubMed |
| Diraviyam K, Stahelin RV, Cho W, Murray D. 2003. Computer modeling of the membrane interaction of FYVE domains. J Mol Biol. 328:721-36. PubMed |
| Kutateladze, T., and Overduin, M. 2001. Structural mechanism of endosome docking by the FYVE domain. Science. 291:1793-1796. PubMed |
| Comments on 1hyi » Early endosome antigen 1 (EEA1), monomer |
|---|
| This orientation is in agreement with results of computational modeling of FYVE domains based on electrostatic interactions (Diraviyam et al. 2003). However, FYVE domain penetrates by ~15A deeper into the membrane according to our results: nonpolar residues are inserted in the membrane hydrocarbon core, not in the head group region. |
