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Structure Prediction: How good are we?

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Presentation on theme: "Structure Prediction: How good are we?"— Presentation transcript:

1 Structure Prediction: How good are we?
R.B. Russell, M.J.E. Sternberg  Current Biology  Volume 5, Issue 5, Pages (May 1995) DOI: /S (95)

2 Figure 1 A comparison of the known and predicted secondary structures of PH domains (the pleckstrin sequence is of its amino-terminal PH domain). From the top, the figure shows: the aligned sequences of three PH domains (white background); the experimentally determined secondary structures (grey background); and the predicted secondary structures (yellow background). Blue arrows indicate β strands, red tubes α helices. The experimentally determined secondary structures were taken from the literature, except in the case of the R.Dynamin X-ray structure, for which Kabsch and Sander's DSSP program [22] was used. The figure was made using the ALSCRIPT program [23]. Current Biology 1995 5, DOI: ( /S (95) )

3 Figure 2 Crystal structure of the dynamin PH domain [11]. β strands are shown as arrows and the α helix as a cylinder. Structures predicted by Musacchio et al.[2] are shown mapped on to the structure: red, β strand; purple, α helix. Current Biology 1995 5, DOI: ( /S (95) )


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