PDB ID or protein name

1dvp » Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)

1dvp » Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)
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Topology in Endosome membrane
Topologylumenal side
cytoplasmic side
1dvp » Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)
Depth 3.0 ± 0.0 Å
Tilt Angle 89 ± 0°
ΔGtransfer -6.6 kcal/mol
Links to 1dvp PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 2.00 Å
Other PDB entries representing this structure none
Number of subunits 2
Experimental Verification for 1dvp » Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)
The dimer probably dissociates or slightly change conformation after interaction with membrane because each monomeric unit tends to interact with the bilayer independently. A symmetric binding mode (Mao et al. (2000) and Diraviyam et al. (2003) has a higher energy. Monomeric FYVE domain has a partially different orientation with respect to the membrane (Blatner et al. 2004).
3 references
Blatner NR, Stahelin RV, Diraviyam K, Hawkins PT, Hong W, Murray D, Cho W. 2004. The molecular basis of the differential subcellular localization of FYVE domains. J Biol Chem. 279:53818-27. 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
Mao Y, Nickitenko A, Duan X, Lloyd TE, Wu MN, Bellen H, Quiocho FA. 2000. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell. 100:447-56. PubMed
Comments on 1dvp » Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)
Essential role in endosome membrane invagination and formation of multivesicular bodies, MVBs. Each monomeric unit in the dimer includes a VHS and a FYVE domain. Additional membrane-anchoring elements: inositol lipids that are specifically bound to FYVE domains.