Bookshelf

Crystal and solution structures of GAG–protein complexes. (A) Crystal structure of the FGF2–hexasaccharide complex (PDB: 1BFC). Key interactions between the hexasaccharide and FGF2 are shown in black dotted lines. The hexasaccharide is shown in stick representation. (B) Crystal structure of the 2:2:2 FGF2–FGFR1–heparin complex (PDB: 1FQ9). FGF2 is shown in salmon, and FGFR1 dimers are shown in green and gold, respectively. Heparin octasaccharides are shown in stick representation. (C) Crystal structure of the 2:2:1 FGF1–FGFR2–heparin complex (PDB: 1E0O). FGF1 dimers are shown in salmon, and FGFR2 dimers are shown in green and gold, respectively. Heparin decasaccharide is shown in stick representation. (D) Model of a CCL5-CS tetrameric complex assembled from the dimeric crystal structure using solution nuclear magnetic resonance (NMR) and small-angle X-ray scattering (SAXS) data. CS hexamers and interacting protein residues are shown as stick figures.

Structures of zinc finger, KH domain and dsRBM in complex with RNA. A) Amino-acid sequences of zinc fingers presented in panels B to E. The residues that interact with the zinc ion are in red. B) Solution structure of Tis11d ZnF1 in complex with the 5′-UAUU-3′ RNA.50 C) Solution structure of the ZnF1 of HIV-1 nucleocapsid protein bound to the 5′-AG-3′ dinucleotide.47 D) Crystal structure of MBNL1 ZnF3 bound to the 5′-GC-3′ dinucleotide.54 E) Crystal structure of ZRANB2 ZnF2 in complex with the 5′-GGU-3′ RNA.52 The zinc atom and water molecules are represented by black and red spheres, respectively. Side chains of residues interacting with the zinc ion are in black. F) Crystal structure of Nova2 KH3 bound to the 5′-UCAC-3′ RNA.67 G) Solution structure of SF1 KH and QUA2 domains in complex with the 5′-ACUAAC-3′ RNA.68 The QUA2 domain is represented in red. H) Solution structure of ADAR2 dsRBM1 in complex with a stem-loop RNA.82 Helix α1 and loop β1-β2 that interact with minor groves are shown in red. Figures were generated by the program MOLMOL90 using the same colour schemes that in the Figure 2.

In the sequence, the KIM is in blue, the PTP domain in green with the PTP signature motif underlined, and the phosphorylation sites in red. In the structure, colors indicate α-helices, β-sheets (left), and surface charge (middle)

In the sequence, the KIM is in blue, the PTP domain in green with the PTP signature motif underlined, and the phosphorylation sites in red. In the structure, colors indicate α-helices, β-sheets (left), and surface charge (middle)