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Figure 1.
Figure 1 Protein interaction domains of IB1. (A) IB1 is
characterized by a JBD (gray box, residues 154–182), SH3
(yellow box, residues 494–553) and a PID (orange box, residues
570–704). Residues are numbered according to the full-length
rat IB1 sequence (GenBank, AF108959). The seven PxxP motifs are
shown in black and red. Motifs marked in red are conserved in
rat, human and mouse IB1 and IB2. MKK7 and MLK3, two of the
known partners of IB1, bind to regions 287–472 and 473–709
of IB1, respectively. (B) Schematic representations of
full-length and C-terminal deletion mutants of IB1. Numbering
corresponds to the last amino-acid expressed in the various
constructs. Binding results described in Figure 2 are summarized
for all constructs. ND: not determined. (C) Sequence alignment
of rat, mouse and human IB1/JIP1 and IB2/JIP2 SH3 domains. The
sequence of rat IB1 (GenBank, AF108959), human JIP1 (Ensembl,
ENSP00000241014), mouse JIP1 (Ensembl, ENSMUSP00000050773), rat
IB2 (Ensembl, ENSRNOP00000050155), human IB2 (GenBank, AF218778)
and mouse JIP2 (Ensembl, ENSMUSP00000023291) are included. The
IB1 SH3 region is identical in all three species. Residues that
participate to IB1 dimerization as well as those expected to do
so in IB2 are shown in bold blue. Residues at the dimer
interface involved in inter-protomer salt bridges or hydrogen
bonds are shaded in green. Nonconserved amino acids between IB1
and IB2 are indicated with a star in the consensus sequence. The
positions of the  strands
1–5 and the 3[10]-helix are indicated in yellow.
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