2HKN

Crystal structure of the CAP-Gly domain of human Dynactin-1 (p150-Glued)

2HKN の概要

• エントリーDOI: 10.2210/pdb2hkn/pdb
• 関連するPDBエントリー: 1TXQ 2COY 2HKQ 2HL3 2HL5
• 分子名称: Dynactin-1 (2 entities in total)
• 機能のキーワード: microtubule binding, cytoskeleton associated protein, p150-glued, strand swap, eb1 and clip-170 binding protein, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q14203
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20618.83

構造登録者

Honnappa, S.,Winkler, F.K.,Steinmetz, M.O. (登録日: 2006-07-05, 公開日: 2006-09-12, 最終更新日: 2024-02-14)

主引用文献

Honnappa, S.,Okhrimenko, O.,Jaussi, R.,Jawhari, H.,Jelesarov, I.,Winkler, F.K.,Steinmetz, M.O.
Key interaction modes of dynamic +TIP networks.
Mol.Cell, 23:663-671, 2006

PubMed Abstract: Dynamic microtubule plus-end tracking protein (+TIP) networks are implicated in all functions of microtubules, but the molecular determinants of their interactions are largely unknown. Here, we have explored key binding modes of +TIPs by analyzing the interactions between selected CAP-Gly, EB-like, and carboxy-terminal EEY/F-COO(-) sequence motifs. X-ray crystallography and biophysical binding studies demonstrate that the beta2-beta3 loop of CAP-Gly domains determines EB-like motif binding specificity. They further show how CAP-Gly domains serve as recognition domains for EEY/F-COO(-) motifs, which represent characteristic and functionally important sequence elements in EB, CLIP-170, and alpha-tubulin. Our findings provide a molecular basis for understanding the modular interaction modes between alpha-tubulin, CLIPs, EB proteins, and the dynactin-dynein motor complex and suggest that multiple low-affinity binding sites in different combinations control dynamic +TIP networks at microtubule ends. They further offer insights into the structural consequences of genetic CAP-Gly domain defects found in severe human disorders.

PubMed: 16949363
DOI: 10.1016/j.molcel.2006.07.013

実験手法

X-RAY DIFFRACTION (1.87 Å)