Anopheles gambiae PGRPLC-Mediated Defense against Bacteria Modulates Infections with Malaria Parasites (original) (raw)
Figure 6
TCT-mediated hetero-dimerization of Anopheles PGRPLC isoforms.
Heterodimer models of _Ag_PGRPLC1-TCT-LC2 (A), _Ag_PGRPLC1-TCT-LC3 (B), _Ag_PGRPLC2-TCT-LC1 (C) and _Ag_PGRPLC2-TCT-LC3 (D). PGRPLC/x molecules are shown in molecular surface models and PGRPLC/a in ribbon diagrams. The PGRPLC/a N-terminus and helix α2 that mediate dimerization are indicated, with monomer-interacting parts colored in orange, parts contacting both monomer and TCT in green and the TCT-interacting part in pink. Interface residues on the surface of PGRPLC/x are shown in blue. (E) Detail alignment of the PD-loop between Ag and Dm PGRPLCs, highlighting the modeled loop and clashing residues. (F) Stereo view of the putative dimer interface at the contact between helix α2/PD-loop of _Ag_PGRPLC3/x and helix α2 of _Ag_PGRPLC1/a (pale green). Three alternative _Ag_PGRPLC3/x models corresponding to different PD-loop modeling approaches are superimposed; in grey the model from MODELLER, in gold the average model structure from ARIA; and in turquoise the Robetta model. PD-loop Residues D61 and S62 (magenta), which clash severely with helix a2 in the three models, and the anchor, TCT-interacting residues R63 and F65, are shown in sticks.