For secondary transporters, one of my current favorite reviews on this
and related is:
Forrest, Kramer & Ziegler, "The structural basis of secondary active
transport mechanisms." Biochim Biophys Acta. 2011, 1807(2)
http://www.ncbi.nlm.nih.gov/pubmed/21029721
Don't know if it is specific enough for what you need, but might be a start.
hth
/Bjorn
--
Bjørn Panyella Pedersen, PhD
Macromolecular Structure Group
Dept. of Biochemistry and Biophysics
University of California, San Francisco
MC2240, 600 - 16th Street S414
San Francisco, CA 94158-2517
Phone: +1 415-476-3937
E-mail: [email protected]
http://www.msg.ucsf.edu
On 05/05/2014 10:31 AM, Keller, Jacob wrote:
Dear Crystallographers (teleology-haters exempt here),
Does anyone know of any references discussing teleology of inverted repeats in
transporters, i.e., what design sense does it make to use this architecture,
why is it so common even in the absence of sequence similarity? Is there some
underlying feature of this general design principle that helps transporters
work well? I suspect someone has discussed it somewhere?
Similarly, generally, with regard to oligomers, which are so common: what's the
advantage? Isn't it just as likely to generate a protein-protein interface of
proteins AB as making an AA interface? Or perhaps it's not? It just seems to me
that oligomerization is way too over-represented in the structural world to be
by chance.
All the best,
Jacob
*******************************************
Jacob Pearson Keller, PhD
Looger Lab/HHMI Janelia Farms Research Campus
19700 Helix Dr, Ashburn, VA 20147
email: [email protected]
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