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5YBV

The structure of the KANK2 ankyrin domain with the KIF21A peptide

Summary for 5YBV
Entry DOI10.2210/pdb5ybv/pdb
DescriptorKN motif and ankyrin repeat domain-containing protein 2, Kinesin-like protein KIF21A, SULFATE ION, ... (6 entities in total)
Functional Keywordscell adhesion
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm: Q63ZY3 Q63ZY3
Cytoplasm, cytoskeleton : Q7Z4S6
Total number of polymer chains4
Total formula weight62311.13
Authors
Guo, Q.,Liao, S.,Min, J.,Xu, C.,Structural Genomics Consortium (SGC) (deposition date: 2017-09-05, release date: 2017-12-06, Last modification date: 2023-11-22)
Primary citationGuo, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.12 Å)
Structure validation

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数据于2025-07-02公开中

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