4TTO

Quasi-racemic structure of [V25A] kalata B1

4TTO の概要

• エントリーDOI: 10.2210/pdb4tto/pdb
• 分子名称: Kalata-B1, D-kalata B1 (3 entities in total)
• 機能のキーワード: cyclic peptide, disulfide bonds, plant protein
• 由来する生物種: Oldenlandia affinis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 5806.64

構造登録者

Wang, C.K.,King, G.J.,Craik, D.J. (登録日: 2014-06-22, 公開日: 2014-09-10, 最終更新日: 2024-11-13)

主引用文献

Wang, C.K.,King, G.J.,Northfield, S.E.,Ojeda, P.G.,Craik, D.J.
Racemic and Quasi-Racemic X-ray Structures of Cyclic Disulfide-Rich Peptide Drug Scaffolds.
Angew.Chem.Int.Ed.Engl., 53:11236-11241, 2014

PubMed 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.

PubMed: 25168664
DOI: 10.1002/anie.201406563

実験手法

X-RAY DIFFRACTION (2.3002 Å)