journal menu
![[Figure 3]](ni5026fig3mag.jpg)
|
|
Figure 3
(a) The binding sites of nine fragments on the hBRR2T1–hJab1ΔC complex. The crystal structures of the fragment complexes were aligned with the crystal structure of unliganded hBRR2T1–hJab1ΔC (PDB entry 6s8q), and only the unliganded hBRR2T1–hJab1ΔC structure is shown as a cartoon for clarity. Pocket 1 corresponds to part of the sulfaguanidine binding site in isolated hBRR2T1 and is bound by fragments 18, 26, 34 and 39. Pocket 2 is located in the N-terminal RecA1 domain and is bound by fragments 18, 34 and 39 (pose 1) and fragments 76, 78 and 86 (pose 2). Pocket 3 is located at the interface between the cassettes at a distance of approximately 21 Å from pocket 1 and is bound by fragments 24 and 50. Pocket 4 corresponds to the ATP-binding pocket of the CC and is bound by fragment 18. Pocket 5 is located on the surface of hBRR2T1 at the N-terminal RecA1 domain and is bound by compound 26. Pocket 6 is positioned at the interface between the N-terminal IG domain of hBRR2T1 and hJab1ΔC and is bound by fragment 39. Fragments are shown as sticks and coloured by atom type as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} (c), except that fragment C atoms are coloured by fragment. (b) FTMap results for isolated hBRR2T1 (PDB entry 4f91; grey cartoon). The FTMap server was used to predict the binding of probes to the crystal structure of isolated hBRR2T1. Probes that bind to the same site form a cluster (C1–C13, clusters 1–13). The clusters are ranked according to the number of predicted interacting probe molecules, with lower cluster numbers corresponding to a larger number of probes. Numbers of interacting probes are indicated in parentheses. Predicted interacting probe molecules are shown as sticks and coloured by atom type as in Fig. 1(c), except that probe molecule C atoms are coloured by probe molecule. (c) FTMap results for the hBRR2T1–hJab1ΔC complex (PDB entry 6s8q; hBRR2T1, grey cartoon; hJab1ΔC, dark grey cartoon). Clusters and bound probes are shown and labelled as in (b). (d) Comparison of predicted hot spots and identified fragment-binding pockets. The structures of all hBRR2T1–hJab1ΔC–fragment complexes were aligned with the unliganded hBRR2T1–hJab1ΔC complex structure including the FTMap-predicted clusters. Interacting fragments and FTMap-predicted interacting probe molecules are shown as sticks. Interacting fragments, cyan; FTMap-predicted interacting probe molecules, magenta. Fragment-binding pockets are labelled as in (a) and clusters are labelled as in (c). |
![[Figure 3]](ni5026fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
