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![[Figure 3]](nj5292fig3mag.jpg)
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Figure 3
The initiating methionine (Met0) in the Met CXCL13 structure mediates both intermolecular and intramolecular interactions. Structural features are labeled. (a) The Met0 residues in the dimer seen in Fig. 2 ![[link]](../../../../../../logos/arrows/d_arr.gif) (c) (depicted in brick red) form intermolecular hydrogen bonds with Tyr6 (depicted in gold) in symmetry mates within the unit cell. Hydrogen-bond distances (in Å) are provided. (b) Stereoscopic image showing that the initiating methionine (depicted in blue) is stabilized by a hydrophobic groove in the core domain established by amino-acid residues Leu2, Ile26, Ile29, Met65 and Leu69 (depicted as red sticks). The hydrophobicity was determined using the normalized consensus hydrophobicity scale (Eisenberg et al., 1984), in which red and white represent hydrophobic and hydrophilic amino acids, respectively. The surface of the protein (minus the initiating methionine) is shown as a mesh. |
![[Figure 3]](nj5292fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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