5N99

CRYSTAL STRUCTURE OF STREPTAVIDIN with cyclic peptide NQpWQ

5N99 の概要

• エントリーDOI: 10.2210/pdb5n99/pdb
• 分子名称: Streptavidin, ASN-GLN-DPR-TRP-GLN (3 entities in total)
• 機能のキーワード: streptavidin, biotin binding, d-amino acid, streptavidin cyclic peptide complex, biotin binding protein
• 由来する生物種: Streptomyces avidinii; 詳細
• 細胞内の位置: Secreted: P22629
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 234256.46

構造登録者

Lyamichev, V.,Goodrich, L.,Sullivan, E.,Bannen, R.,Benz, J.,Albert, T.,Patel, J. (登録日: 2017-02-24, 公開日: 2017-10-04, 最終更新日: 2024-11-20)

主引用文献

Lyamichev, V.I.,Goodrich, L.E.,Sullivan, E.H.,Bannen, R.M.,Benz, J.,Albert, T.J.,Patel, J.J.
Stepwise Evolution Improves Identification of Diverse Peptides Binding to a Protein Target.
Sci Rep, 7:12116-12116, 2017

PubMed Abstract: Considerable efforts have been made to develop technologies for selection of peptidic molecules that act as substrates or binders to a protein of interest. Here we demonstrate the combination of rational peptide array library design, parallel screening and stepwise evolution, to discover novel peptide hotspots. These hotspots can be systematically evolved to create high-affinity, high-specificity binding peptides to a protein target in a reproducible and digitally controlled process. The method can be applied to synthesize both linear and cyclic peptides, as well as peptides composed of natural and non-natural amino acid analogs, thereby enabling screens in a much diverse chemical space. We apply this method to stepwise evolve peptide binders to streptavidin, a protein studied for over two decades and report novel peptides that mimic key interactions of biotin to streptavidin.

PubMed: 28935886
DOI: 10.1038/s41598-017-12440-1

実験手法

X-RAY DIFFRACTION (1.5 Å)