Hi Shane, One example that comes to mind is aquaporin-z. Two protomers were found in the ASU, one contained the water channel in an open conformation while the other in a closed conformation. The structural differences are not “large” but the functional implication is.
Here is the primary citation Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z. Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD 3rd, Stroud RM. PLoS Biol. 2003 Dec;1(3):E72. Epub 2003 Dec 22. Kind regards Tamir —— gon...@hhmi.org On Jan 27, 2014, at 1:08 PM, Shane Caldwell <shane.caldwel...@gmail.com> wrote: > Hi ccp4bb, > > I'm putting together a talk for some peers that highlights strengths and > weaknesses of structural models for the outsider. For one point, I'd like to > find some examples of proteins that show very different conformations between > different copies in the ASU. One example I know of is c-Abl (1OPL), which > crystallizes with both autoinhibited and active forms in the ASU, with > dramatically different domain organization. I'd like to find some additional > examples - can anyone suggest some other structures that have multiple copies > with large structural variations? > > Thanks in advance! > > Shane Caldwell > McGill University > >
