8FRF

Homodimeric designed loop protein RBL7_C2_3

8FRF の概要

• エントリーDOI: 10.2210/pdb8frf/pdb
• 分子名称: RBL7_C2_3, MALONATE ION (3 entities in total)
• 機能のキーワード: designed protein, helical repeat, homodimer, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 187192.88

構造登録者

Jude, K.M.,Jiang, H.,Baker, D.,Garcia, K.C. (登録日: 2023-01-06, 公開日: 2024-04-17, 最終更新日: 2024-08-07)

主引用文献

Jiang, H.,Jude, K.M.,Wu, K.,Fallas, J.,Ueda, G.,Brunette, T.J.,Hicks, D.R.,Pyles, H.,Yang, A.,Carter, L.,Lamb, M.,Li, X.,Levine, P.M.,Stewart, L.,Garcia, K.C.,Baker, D.
De novo design of buttressed loops for sculpting protein functions.
Nat.Chem.Biol., 20:974-980, 2024

PubMed Abstract: In natural proteins, structured loops have central roles in molecular recognition, signal transduction and enzyme catalysis. However, because of the intrinsic flexibility and irregularity of loop regions, organizing multiple structured loops at protein functional sites has been very difficult to achieve by de novo protein design. Here we describe a solution to this problem that designs tandem repeat proteins with structured loops (9-14 residues) buttressed by extensive hydrogen bonding interactions. Experimental characterization shows that the designs are monodisperse, highly soluble, folded and thermally stable. Crystal structures are in close agreement with the design models, with the loops structured and buttressed as designed. We demonstrate the functionality afforded by loop buttressing by designing and characterizing binders for extended peptides in which the loops form one side of an extended binding pocket. The ability to design multiple structured loops should contribute generally to efforts to design new protein functions.

PubMed: 38816644
DOI: 10.1038/s41589-024-01632-2

実験手法

X-RAY DIFFRACTION (2.99 Å)