{PDOC51776} {PS51776; RH1} {BEGIN} ********************** * RH1 domain profile * ********************** The RH1 (RILP homology 1) protein-protein interaction domain is found in the following animal Rab36-binding proteins: - Rab interacting lysosomal proteins (RILP), - RILP-like 1 (RILP-L1), - RILP-like 2 (RILP-L2), - JNK-interacting protein 3 (JIP3), - JNK-interacting protein 4 (JIP4). It binds to the myosin Va globular tail domain (MyoVa-GTD) in mainly hydrophobic interactions. The RH1 domain adopts an all-helical structure (see ) and forms a homodimer with a four-helix bundle conformation to interact with MyoVa-GTD. The RH1 homodimer is structurally separated into two parts, the N-terminal four-helix bundle formed by alpha2 and alpha3N and the C-terminal coiled-coil formed by alpha3C. The four-helix bundle in the RH1 dimer is mainly stabilized by forming a hydrophobic core. The N-terminal small helix (alpha1) and its following loop pack on alpha2 from the same molecule and alpha3 from the neighboring molecule and thus contribute to the bundle stability. The RH1 homodimer is further strengthened by a coiled coil formed by the C-terminal half of the alpha3-helix [1]. The profile we developed covers the entire RH1 domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: October 2015 / First entry. [ 1] Wei Z., Liu X., Yu C., Zhang M. "Structural basis of cargo recognitions for class V myosins." Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013). PubMed=23798443; DOI=10.1073/pnas.1306768110 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}