5YBV

The structure of the KANK2 ankyrin domain with the KIF21A peptide

5YBV の概要

• エントリーDOI: 10.2210/pdb5ybv/pdb
• 分子名称: KN motif and ankyrin repeat domain-containing protein 2, Kinesin-like protein KIF21A, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm: Q63ZY3 Q63ZY3; Cytoplasm, cytoskeleton : Q7Z4S6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62311.13

構造登録者

Guo, Q.,Liao, S.,Min, J.,Xu, C.,Structural Genomics Consortium (SGC) (登録日: 2017-09-05, 公開日: 2017-12-06, 最終更新日: 2023-11-22)

主引用文献

Guo, Q.,Liao, S.,Zhu, Z.,Li, Y.,Li, F.,Xu, C.
Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins.
J. Biol. Chem., 293:557-566, 2018

PubMed Abstract: A well-controlled microtubule organization is essential for intracellular transport, cytoskeleton maintenance, and cell development. KN motif and ankyrin repeat domain-containing protein 1 (KANK1), a member of KANK family, recruits kinesin family member 21A (KIF21A) to the cell cortex to control microtubule growth via its C-terminal ankyrin domain. However, how the KANK1 ankyrin domain recognizes KIF21A and whether other KANK proteins can also bind KIF21A remain unknown. Here, using a combination of structural, site-directed mutagenesis, and biochemical studies, we found that a stretch of ∼22 amino acids in KIF21A is sufficient for binding to KANK1 and its close homolog KANK2. We further solved the complex structure of the KIF21A peptide with either the KANK1 ankyrin domain or the KANK2 ankyrin domain. In each complex, KIF21A is recognized by two distinct pockets of the ankyrin domain and adopts helical conformations upon binding to the ankyrin domain. The elucidated KANK structures may advance our understanding of the role of KANK1 as a scaffolding molecule in controlling microtubule growth at the cell periphery.

PubMed: 29183992
DOI: 10.1074/jbc.M117.817494

実験手法

X-RAY DIFFRACTION (2.12 Å)