From mmconn-!at!-silibone.cchem.berkeley.edu  Wed Nov 29 13:39:04 1995
Received: from hydrogen.CChem.Berkeley.EDU  for mmconn#* at *#silibone.cchem.berkeley.edu
	by www.ccl.net (8.6.10/950822.1) id NAA15973; Wed, 29 Nov 1995 13:32:52 -0500
Received: from silibone.cchem.berkeley.edu by hydrogen.CChem.Berkeley.EDU (8.6.10/1.41)
	id KAA12174; Wed, 29 Nov 1995 10:32:52 -0800
Received: by silibone.cchem.berkeley.edu (920330.SGI/920502.SGI.AUTO)
	for  # - at - # hydrogen.cchem.berkeley.edu:chemistry # - at - # www.ccl.net id AA15628; Wed, 29 Nov 95 10:29:12 -0800
Date: Wed, 29 Nov 95 10:29:12 -0800
From: mmconn:~at~:silibone.cchem.berkeley.edu (morgan conn)
Message-Id: <9511291829.AA15628%!at!%silibone.cchem.berkeley.edu>
To: chemistry%!at!%www.ccl.net
Subject: binding pocket?



Hello all;

I'm looking for the impossible.

If I have an inhibitor and a protein that are known to associate, and a set
of mutations that appear to reduce the in vivo effects of this small molecule,
is there a way to (reasonably) find a binding pocket for this molecule on the
protein surface? The normal substrate for the molecule shows little, if any,
structural similarity to the inhibitor, so the the substrate pocket would 
_not_ seem to be the binding site. 

Does anyone have experience/knowledge of this sort of thing.          


-morgan



********************************************************************
        Dr. M. Morgan Conn
        Department of Chemistry (Schultz group), UC Berkeley
        mmconn _-at-_)silibone.cchem.berkeley.edu
        510.642.9249; 510.643.6890 (fax)
********************************************************************