5ybv

The structure of the KANK2 ankyrin domain with the KIF21A peptide

spinqualitylabelsall models 5ybv, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ybv is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.12Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KANK2_HUMAN Involved in transcription regulation by sequestering nuclear receptor coactivators, such as NCOA1, NCOA2 and NCOA3, in the cytoplasm; the function is deregulated by phosphorylation. May be involved in the control of cytoskeleton formation by regulating actin polymerization. Involved in regulation of caspase-independent apoptosis; proposed to sequester AIFM1 in mitochondria and apoptotic stimuli lead to its proteasomal degradation allowing the release of AIFM1 to the nucleus. May be involved in promotion of cell proliferation. Publication Abstract from PubMed 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, could recruit 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, and 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 the role of KANK1 as a scaffolding molecule in controlling microtubule growth at the cell periphery. Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins.,Guo Q, Liao S, Zhu Z, Li Y, Li F, Xu C J Biol Chem. 2017 Nov 28. pii: M117.817494. doi: 10.1074/jbc.M117.817494. PMID:29183992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ankyrin repeat domain-containing protein Ankyrin repeat domain-containing protein 3D structures

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