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Figure 3.
Figure 3. Electron density of the HMC-L-Pro[15] peptide and the
asymmetric unit of the HPP−HMC-L-Pro[15] complex. a,
Refined HMC-L-Pro[15] coordinates with 2.3 Å 2F[o] - F[c]
electron density (blue). Peptide orientation was unambiguously
defined by density corresponding to the N-terminal HMC moiety.
The five aromatic residues that comprise the proline-rich
peptide binding core and three additional residues from the
extended binding site are highlighted in red. b, The asymmetric
unit of the HPP−HMC-L-Pro[15] crystal contains two
HPP−peptide complexes related by two-fold non-crystallographic
symmetry. The five aromatic residues that define the minimal
poly-L-proline binding site are shown in red for HPP-1. This
figure was generated using SETOR^31.
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