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PDBsum entry 4ttl
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References listed in PDB file
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Key reference
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Title
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Racemic and quasi-Racemic X-Ray structures of cyclic disulfide-Rich peptide drug scaffolds.
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Authors
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C.K.Wang,
G.J.King,
S.E.Northfield,
P.G.Ojeda,
D.J.Craik.
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Ref.
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Angew Chem Int Ed Engl, 2014,
53,
11236-11241.
[DOI no: ]
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PubMed id
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Abstract
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Cyclic disulfide-rich peptides have exceptional stability and are promising
frameworks for drug design. We were interested in obtaining X-ray structures of
these peptides to assist in drug design applications, but disulfide-rich
peptides can be notoriously difficult to crystallize. To overcome this
limitation, we chemically synthesized the L- and D-forms of three prototypic
cyclic disulfide-rich peptides: SFTI-1 (14-mer with one disulfide bond), cVc1.1
(22-mer with two disulfide bonds), and kB1 (29-mer with three disulfide bonds)
for racemic crystallization studies. Facile crystal formation occurred from a
racemic mixture of each peptide, giving structures solved at resolutions from
1.25 Å to 1.9 Å. Additionally, we obtained the quasi-racemic structures of
two mutants of kB1, [G6A]kB1, and [V25A]kB1, which were solved at a resolution
of 1.25 Å and 2.3 Å, respectively. The racemic crystallography approach
appears to have broad utility in the structural biology of cyclic peptides.
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