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Figure 4.
Figure 4. (a) Peptide binding region of the HckSH3:PD1 complex.
HckSH3 backbone, hydrophobic and aromatic side-chains are
coloured in blue, charged side-chains of HckSH3 are coloured in
red. PD1 peptide backbone, hydrophobic and aromatic side-chains
are coloured in green and Lys3 is highlighted in purple. Polar
amino acid side-chains of PD1 are coloured in grey. The PD1
amino acid sequence, numbering and SH3 binding positions are
shown below. (b) A focus on the anchor residues binding pocket
shows the positions of the peptide residue Lys3 in different
conformers calculated for the HckSH3:PD1 complex. Side-chains
of different PD1 Lys3 conformers are coloured in purple. The
Lys3 side-chain position upon structure calculation employing
additional constraints describing a salt-bridge between Lys3
and D95 is highlighted in orange. (c) View on the RT loop
regions of the HckSH3:PD1 and the FynSH3:3BP2 (PDB code
1FYN^59) complexes. Superposition is based on optimal fitting of
the C^α coordinates within the β-sheets. The conserved
tryptophan (HckSH3 residue W113) and proline side-chains as well
as the tyrosine side-chain within the 3[10] helix (HckSH3
residue Y131) are coloured in blue and orange for HckSH3 and
FynSH3, respectively. The conserved tryptophan residue in
the FynSH3 complex structure (W119) is known to adopt a SH3-I
orientation.^58 Compared to Fyn W119, the plane of the HckSH3
W113 side-chain is tilted by about 12° towards the conserved
proline residue, indicating a SH3-II orientation for W113 in
the HckSH3:PD1 complex structure. Figure 4. (a) Peptide
binding region of the HckSH3:PD1 complex. HckSH3 backbone,
hydrophobic and aromatic side-chains are coloured in blue,
charged side-chains of HckSH3 are coloured in red. PD1 peptide
backbone, hydrophobic and aromatic side-chains are coloured in
green and Lys3 is highlighted in purple. Polar amino acid
side-chains of PD1 are coloured in grey. The PD1 amino acid
sequence, numbering and SH3 binding positions are shown below.
(b) A focus on the anchor residues binding pocket shows the
positions of the peptide residue Lys3 in different conformers
calculated for the HckSH3:PD1 complex. Side-chains of different
PD1 Lys3 conformers are coloured in purple. The Lys3 side-chain
position upon structure calculation employing additional
constraints describing a salt-bridge between Lys3 and D95 is
highlighted in orange. (c) View on the RT loop regions of the
HckSH3:PD1 and the FynSH3:3BP2 (PDB code 1FYN[3]^59) complexes.
Superposition is based on optimal fitting of the C^α
coordinates within the β-sheets. The conserved tryptophan
(HckSH3 residue W113) and proline side-chains as well as the
tyrosine side-chain within the 3[10] helix (HckSH3 residue Y131)
are coloured in blue and orange for HckSH3 and FynSH3,
respectively. The conserved tryptophan residue in the FynSH3
complex structure (W119) is known to adopt a SH3-I
orientation.[4]^58 Compared to Fyn W119, the plane of the HckSH3
W113 side-chain is tilted by about 12° towards the conserved
proline residue, indicating a SH3-II orientation for W113 in the
HckSH3:PD1 complex structure.
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