2WOZ

The novel beta-propeller of the BTB-Kelch protein Krp1 provides the binding site for Lasp-1 that is necessary for pseudopodia extension

2WOZ の概要

• エントリーDOI: 10.2210/pdb2woz/pdb
• 分子名称: KELCH REPEAT AND BTB DOMAIN-CONTAINING PROTEIN 10 (2 entities in total)
• 機能のキーワード: protein binding, invasion and metastasis, ubl conjugation pathway, ubl protein folding, cell projection, cytoskeleton, kelch repeat, kelch domain
• 由来する生物種: RATTUS NORVEGICUS (RAT)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35418.43

構造登録者

Gray, C.H.,McGarry, L.C.,Spence, H.J.,Riboldi-Tunnicliffe, A.,Ozanne, B.W. (登録日: 2009-07-31, 公開日: 2009-09-01, 最終更新日: 2024-05-08)

主引用文献

Gray, C.H.,McGarry, L.C.,Spence, H.J.,Riboldi-Tunnicliffe, A.,Ozanne, B.W.
Novel beta-propeller of the BTB-Kelch protein Krp1 provides a binding site for Lasp-1 that is necessary for pseudopodial extension.
J. Biol. Chem., 284:30498-30507, 2009

PubMed Abstract: Kelch-related protein 1 (Krp1) is up-regulated in oncogene-transformed fibroblasts. The Kelch repeats interact directly with the actin-binding protein Lasp-1 in membrane ruffles at the tips of pseudopodia, where both proteins are necessary for pseudopodial elongation. Herein, we investigate the molecular basis for this interaction. Probing an array of overlapping decapeptides of Rattus norvegicus (Rat) Krp1 with recombinant Lasp-1 revealed two binding sites; one ((317)YDPMENECYLT(327)) precedes the first of five Kelch repeats, and the other ((563)TEVNDIWKYEDD(574)) is in the last of the five Kelch repeats. Mutational analysis established that both binding sites are necessary for Krp1-Lasp-1 interaction in vitro and function in vivo. The crystal structure of the C-terminal domain of rat Krp1 (amino acids 289-606) reveals that both binding sites are brought into close proximity by the formation of a novel six-bladed beta-propeller, where the first blade is not formed by a Kelch repeat.

PubMed: 19726686
DOI: 10.1074/jbc.M109.023259

実験手法

X-RAY DIFFRACTION (2 Å)