The FASEB Journal, Vol 10, 927-930, Copyright © 1996 by The Federation of American Societies for Experimental Biology

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Collagen/collagenase interaction: does the enzyme mimic the conformation of its own substrate?

SJ De Souza, HM Pereira, S Jacchieri and RR Brentani
Ludwig Institute for Cancer Research, Sao Paulo Branch, Brasil.

In this report, we present a hypothesis on the mechanism used by interstitial collagenases to cleave their natural substrate, interstitial collagens. The hypothesis is based on the assumption that the proline hinge domain of interstitial collagenase adopts a collagen- like conformation. With a collagen-like domain, the enzyme is able to disturb the quaternary organization of the triple helix in the collagenase-susceptible site. A modeling analysis suggests that interaction between prolines of both collagen and collagenase forming a kind of "proline zipper" is involved in the destabilization step. This destabilization makes the three-collagen helix susceptible to the catalytic cleft of the catalytic core.

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