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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

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On Jan 27, 2014, at 1:08 PM, Shane Caldwell <[log in to unmask]> 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