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![[Figure 2]](gi5036fig2mag.jpg)
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Figure 2
Main MagaFab–peptide interactions. (a) The bidentate interaction between the amides of Gln5Pep and Gln50VH, as well as the salt bridges between Lys3Pep and Asp55VH and Asp57VH, are the key interactions that determine the recognition of the peptide by the Fab. Additional weaker interactions and those involving structural waters are also represented by yellow dashed lines. The VH chain is shown in green, the VL chain in orange, the main peptide in purple and the symmetric peptide in pink. (b) The same as (a) but from a different orientation. (c) Stabilization of the nonpolar section of the peptide. The short 310-helix of the peptide is flanked by Trp96VL, while Leu7Pep is located near Val103VH. The carbonyl group of Val6Pep is stabilized by a water located between the hydroxyl group of Ser95VL and the Tyr54VL and Thr102VH carbonyl groups. An interaction with the symmetric peptide is established between Asp10Pep and Asn2Pep*. (d) Stabilization of the peptide 310-helix moiety by symmetry molecules. Lys9Pep, Asp10Pep, Leu11Pep and Gln15Pep are stabilized by Ser206VL, Gly1Pep*, Asn2Pep* and Thr101VH from symmetry molecules (represented in light orange, light pink and light green, respectively). |
![[Figure 2]](gi5036fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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