Here is one like that.
Chaperoned Ubiquitylation—Crystal Structures of the CHIP U Box E3
Ubiquitin Ligase and a CHIP-Ubc13-Uev1a Complex .
Molecular Cell , Volume 20 , Issue 4 , Pages 525 - 538
M . Zhang , M . Windheim , S . Roe , M . Peggie , P . Cohen , C .
Prodromou , L . Pearl
Young-Tae
On Sep 22, 2008, at 9:15 AM, Kornelius Zeth wrote:
Dear all,
I'm searching for examples of crystal structures that show a clear
asymmetry in the dimeric/oligomeric state. This asymmetry should
not have been induced by the crystal packing (e.g. two domains
connected by a long linker packing different, termini/loops which
interact differently with the surrounding) rather than by an
internal asymmetry (which may be confirmed by other techniques e.g.
SAXS).
The reason I'm asking: I have solved a couple of crystal structures
of a chimera protein (110 residues, dimeric, 1.2 A resolution) and
mutants of the same fragment consisting of basically two four helix
bundles and a short connector fragment and these are highly
asymmetric (although the H-bond pattern of the helix residues
doesn't change) while the same structures solved by NMR are
symmetric and largely different. PISA gives a variety of contacts
(H-bonds, salt bridges) between the two chains, interface seems ok,
stable, low B-factors).
Any comments and suggestions are appreciated
Best wishes and thanks!
Kornelius
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Kornelius Zeth
Max Planck Institute for Developmental Biology
Dept. Protein Evolution
Spemannstr. 35
72076 Tuebingen, Germany
[EMAIL PROTECTED]
Tel -49 7071 601 323
Fax -49 7071 601 349
