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 2.6 ± 0.3 Å
Tilt Angle 90 ± 5°
ΔGtransfer -6.5 kcal/mol
Links to 1dvp PDB Sum, SCOP, MSD, OCA, MMDB, Dali
Topology cytoplasmic
Resolution 2.00 Å
Related PDB Sum entries none
Number of subunits 2
Experimental Verification for 1dvp » Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)
Consistent with membrane-binding mode proposed by Mao et al. (2000) and Diraviyam et al. (2003). Monomeric FYVE domain has a partialy different orientation (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, consistent with the calculated membrane-association mode.