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Resolution: standard / high Figure 3.
PONDR® predictions compared to experimental structural determinations for various autoantigens.
(a) La autoantigen (Swiss-Prot: P05455). The shaded box above the plot (residues 231–325) is the region that Jacks et al. [64] determined to be ordered via NMR. The empty boxes (residues 214–230 and residues
326–408) are regions determined to be unstructured or disordered. The inset (PDB:
1OWX; La222-334) shows the conformational flexibility of disordered regions at the amino
and carboxyl terminii of the La fragment. (b) DNA topoisomerase I (Swiss-Prot: P11387). The structure was determined by X-ray methods for a protein-DNA complex (PDB: 1EJ9) encompassing residues 203–765 of DNA topoisomerase I. Residues 634–713 (empty box)
are missing and, therefore, disordered in the structure [65]. The lightly shaded box
at the amino terminus is the region that was determined to be disordered in the references
cited above. (c) Histone H3 (Swiss-Prot: P68431). The structure of chicken H3 in a histone octamer complex (PDB: 2HIO) was determined by X-ray methods for residues 1–135. Residues 1–42 are missing, presumably
due to disorder [66]. (d) Sm D1 (Swiss-Prot: P62314). The structure of a protein complex between Sm D1 (residues 2–119) and Sm D2 was
studied by X-ray methods (PDB: 1B34) [67]. Residues 82–119 from Sm D1 are missing from the structure.
Carl et al. Arthritis Research & Therapy 2005 7:R1360 doi:10.1186/ar1832 |