Hi Phoebe,
Some of the info on Brian Shoichet's site might be of use. Worth a look
at least.
http://shoichetlab.compbio.ucsf.edu/
Anecdotally, I believe that gleevec was rationally designed from a
scaffold which bound one way, but after gleevec had been shown to be
effective, the X-ray structure revealed that it bound 'the wrong way'.
This is however a mismatch of prediction and reality, rather than two
different realities.
Cheers,
Charlie
[EMAIL PROTECTED] wrote:
A biochemist friend asked for examples of cases were a protein was
co-crystallized with or soaked in a ligand that bound in the wrong place
- say, because the ligand used wasn't quite the right one or because
other important ligands were absent.
I'm sure such examples are out there, especially when soaks were done at
high concentrations, but I'm having trouble thinking of concrete examples.
Help?
thanks,
Phoebe Rice
---------------------------------------------------------------------------------------------------------------------------
Phoebe A. Rice
Assoc. Prof., Dept. of Biochemistry & Molecular Biology
The University of Chicago
phone 773 834 1723
fax 773 702 0439
http://bmb.bsd.uchicago.edu/index.html
http://www.nasa.gov/mission_pages/cassini/multimedia/pia06064.html
.
--
Charlie Bond
Professorial Fellow
University of Western Australia
School of Biomedical, Biomolecular and Chemical Sciences
M310
35 Stirling Highway
Crawley WA 6009
Australia
[EMAIL PROTECTED]
+61 8 6488 4406
