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![[Figure 1]](jv5022fig1mag.jpg)
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Figure 1
Crystal structure of the CB and Sp domains. (a) Overall structure of the ADAMTS-5 construct comprising the N-terminal CB domain (β-hairpin and two-rim-like superhelix) and the Sp domain (β-sandwich formed by two antiparallel β-sheets: β1–β10–β3–β8–β7–β6 and β2–β9–β4–β5). (b) Different orientation of the overall structure of the ADAMTS-5 construct, highlighting the CB domain, with the three disulfide bridges and selected amino acids represented as sticks. (c) Close-up view of the flexible loops β7–β8, β3–β4 (orange) and β9–β10, showing some of the electrostatic interactions stabilizing the loop structures. Structural variability of the β3–β4 loop (orange) is shown by the superposition of the three molecules in the crystal asymmetric unit (the dotted segment represents the unmodelled amino-acid residues 765–767 missing in chain C). Figures were generated using PyMOL (Schrödinger). |
![[Figure 1]](jv5022fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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