Dear CCP4bb,

I have a partly specific question, relating to multidomain enzymes.

We have a nice hi-res structure of an enzyme, which comprises domain A 
(non-catalytic) and domain B (enzymatic)

Through the magic of unstimulated in-tray proteolysis, there are one and a half 
copies in the ASU, one full AB and one A half

The second (proteolysed) domain A is jammed in active site B of the full-length 
AB copy. The contacts look glorious and specific but we don't have enough 
sequence variation among homologues to say if interfaces are conserved.

A full-length AB protein would never inhibit another because the AB domain 
arrangement would cause a steric clash.

So my question is - "do you know of any enzyme where it gets proteolysed to 
generate a fragment that goes on to inhibit itself?". I'd prefer answers that 
are about fragments/complexes rather than say a zymogen state. Hope that makes 
sense

Be great if you can tell me of any - not the easiest thing to search for!
Thanks in advance
Andy

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