Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin

A study related to the interaction between anastellin and the third fibronectic (FN) type III domain (III3), which is a key anastellin binding site on FN is reported. The findings from the matrix-assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry indicated that the middle part of III3 became destabilized and protease sensitive upon anastellin binding and hence the stability of III3 appears to be a key factor in anastellin binding.