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The N‐ and C‐terminal ends of RPGR can bind to PDE 6δ
Author(s) -
Fansa Eyad Kalawy,
O'Reilly Nicola J,
Ismail Shehab,
Wittinghofer Alfred
Publication year - 2015
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201541404
Subject(s) - operations research , library science , computer science , engineering
This study shows that the prenylated C‐terminus of RPGR can bind to PDE6δ with high affinity, suggesting two distinct binding sites of the RPGR/PDE6δ complex. The serine residue at the −3 position relative to the prenylated cysteine seems to play a key role in defining the selectivity of PDE6δ towards ciliary prenylated cargo.