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Fig. 1. (A) Domain structure comparison of AmphiTrk, vertebrate Trk receptors
(TrkA, TrkB and TrkC) and representative invertebrate Trk-like proteins from
Lymnaea stagnalis (LTrk) and Drosophila melanogaster (DTrk).
Modules are colour coded: yellow, Cys-rich clusters; green, leucine-rich
domains; blue, type C2 IgG domains; grey, transmembrane domain; red,
tyrosine-kinase domain; purple, N-terminal extension; turquoise; type V2 IgG
domains. (B) AmphiTrk amino acid sequence. Amino acid positions are numbered
on the left. The putative signal sequence cleavage site is indicated by an
arrowhead. Leucine-rich motifs are in italics and flanking cysteine clusters
in bold. Both Ig-like domains are underlined; conserved asparagines with
structural roles for ligand binding are indicated by dots. The transmembrane
region is underlined by a dotted line. The first phosphorylation site by
cAMP/cGMP-dependent kinase proteins, KIS, is shown with a black background, as
is the tyrosine responsible for Shc recruitment. Within the tyrosine kinase
domain (boxed), the lysine responsible for ATP binding and the second
phosphorylation site by cAMP/cGMP-dependent kinase proteins, RKFT, are shown
by a black background. The autophosphorylation sequence (DIYSTDYYR) is
highlighted in grey and the autophosphorylated tyrosines are shown by a black
background. Glutamine located in the same position as the vertebrate docking
site for PLC
is shown by a black background. AmphiTrk
sequences have been deposited in the GeneBank under Accession Numbers
AY902361-AY902364
