PDBsum entry 4ttl

Toxin

PDB id

4ttl

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Contents

			Protein chain

					22 a.a.

			Waters ×21

PDB id:

4ttl

Links

Name:

Toxin

Title:

Racemic structure of cyclic vc1.1 (cvc1.1-1)

Structure:

Alpha-conotoxin vc1a. Chain: a. Synonym: alpha-vc1a,vc1.1. Engineered: yes

Source:

Synthetic: yes. Conus victoriae. Queen victoria cone. Organism_taxid: 319920

Resolution:

1.70Å

R-factor:

0.193

R-free:

0.226

Authors:

C.K.Wang,G.J.King,D.J.Craik

Key ref:

C.K.Wang et al. (2014). Racemic and quasi-racemic X-ray structures of cyclic disulfide-rich peptide drug scaffolds. Angew Chem Int Ed Engl, 53, 11236-11241. PubMed id: 25168664 DOI: 10.1002/anie.201406563

Date:

22-Jun-14

Release date:

10-Sep-14

PROCHECK

	Headers

	References

Protein chain

P69747 (CA1A_CONVC) - Alpha-conotoxin Vc1a from Conus victoriae

Seq: Struc:					66 a.a. 22 a.a.

Key:

PfamA domain

Secondary structure

DOI no: 10.1002/anie.201406563	Angew Chem Int Ed Engl 53:11236-11241 (2014)
PubMed id: 25168664

Racemic and quasi-racemic X-ray structures of cyclic disulfide-rich peptide drug scaffolds.
C.K.Wang, G.J.King, S.E.Northfield, P.G.Ojeda, D.J.Craik.

ABSTRACT

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.