Structure prediction: Folding proteins by pattern recognition David Shortle  Current Biology  Volume 7, Issue 3, Pages R151-R154 (March 1997) DOI: 10.1016/S0960-9822(97)70076-9

Figure 1 The result of fold recognition with the target exfoliative toxin A from Staphylococcus aureus. (a) The predicted structure of toxin A, based on the structure of the model protein human leukocyte elastase. (b) The crystal structure of the region of human leukocyte elastase predicted to be the best model for toxin A. It was reported at the meeting that human leukocyte elastase (218 amino acids) was the best hit on threading [7] the sequence of toxin A (242 amino acids) through a library of structure-containing representatives of all known fold families. The level of sequence identity is 16%; 152 out of 166 equivalent residue pairs were correctly aligned in the threaded model of toxin A. (Image courtesy of Manfred Sippl.) Current Biology 1997 7, R151-R154DOI: (10.1016/S0960-9822(97)70076-9)