Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations

<table>Two homodimers of the mTS-dUMP-Raltitrexed complex structure, AB and CD, in the asymmetric unit. Subunits A, B, C, and D are colored differently and labeled. The ligands, dUMP and Raltitrexed, are colored according to atom identity (carbon in black, oxygen in red, nitrogen in blue, and sulfur and phosphorus in yellow), shown as sticks, and labeled in subunit D. N- and C-termini are labeled in all subunits. The enzyme belongs to the class of <i>α</i> and <i>β</i> proteins (<i>α</i> + <i>β</i>), with the dimer subunits separated by two reversely symmetrical large mixed <i>β</i>-sheets.</table>

BioMed Research International

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Figure 1: Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations 

Figure 1 | Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations 