pubmed.ncbi.nlm.nih.gov

Assessment of disorder predictions in CASP6 - PubMed

. 2005:61 Suppl 7:167-175.

doi: 10.1002/prot.20734.

Affiliations

Assessment of disorder predictions in CASP6

Yumi Jin et al. Proteins. 2005.

Abstract

Natively disordered proteins or protein segments are those without stable secondary or tertiary structure in the absence of binding partners. Such disordered regions often are important functional sites in many biological processes, especially those involved in transcription, translation, and cell signaling. The prediction of such regions is therefore of great importance in focusing experimental efforts on regions of proteins that may be critical for function. In CASP6, held in 2004, twenty research groups participated in the prediction of disordered regions. Both binary predictions (ordered or disordered) and assigned scores for disorder were assessed. Several groups performed quite well in predicting regions of disorder in the X-ray and NMR structures available to the assessors. The best of these groups performed better than the best groups in CASP5, held in 2002.

2005 Wiley-Liss, Inc.

PubMed Disclaimer

Similar articles

Cited by

References

REFERENCES

    1. Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005; 6: 197-208.
    1. Fink AL. Natively unfolded proteins. Curr Opin Struct Biol 2005; 15: 35-41.
    1. Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004; 337: 635-645.
    1. Iakoucheva LM, Dunker AK. Order, disorder, and flexibility: prediction from protein sequence. Structure (Camb) 2003; 11: 1316-1317.
    1. Gunasekaran K, Tsai CJ, Nussinov R. Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J Mol Biol 2004; 341: 1327-1341.

Publication types

MeSH terms

LinkOut - more resources