9CCE

structure of DYNA_1b7

9CCE の概要

• エントリーDOI: 10.2210/pdb9cce/pdb
• 分子名称: DYNA_1b7, Dynorphin A(1-17) (2 entities in total)
• 機能のキーワード: de novo design, deep learning, disorder peptide, protein-peptide complex, de novo protein
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 54696.10

構造登録者

Bera, A.K.,Wu, K.,Kang, A.,Baker, D. (登録日: 2024-06-21, 公開日: 2025-08-13)

主引用文献

Wu, K.,Jiang, H.,Hicks, D.R.,Liu, C.,Muratspahic, E.,Ramelot, T.A.,Liu, Y.,McNally, K.,Kenny, S.,Mihut, A.,Gaur, A.,Coventry, B.,Chen, W.,Bera, A.K.,Kang, A.,Gerben, S.,Lamb, M.Y.,Murray, A.,Li, X.,Kennedy, M.A.,Yang, W.,Song, Z.,Schober, G.,Brierley, S.M.,O'Neill, J.,Gelb, M.H.,Montelione, G.T.,Derivery, E.,Baker, D.
Design of intrinsically disordered region binding proteins.
Science, 389:eadr8063-eadr8063, 2025

PubMed Abstract: Intrinsically disordered proteins and peptides play key roles in biology, but a lack of defined structures and high variability in sequence and conformational preferences have made targeting such systems challenging. We describe a general approach for designing proteins that bind intrinsically disordered protein regions in diverse extended conformations with side chains fitting into complementary binding pockets. We used the approach to design binders for 39 highly diverse unstructured targets, including polar targets, and obtained designs with 100-picomolar to 100-nanomolar affinities in 34 cases, testing ~22 designs per target. The designs function in cells and as detection reagents and are specific for their intended targets in all-by-all binding experiments. Our approach is a major step toward a general solution to the intrinsically disordered protein and peptide recognition problem.

PubMed: 40674483
DOI: 10.1126/science.adr8063

実験手法

X-RAY DIFFRACTION (3.15 Å)