4O6X

Crystal structure of human Ankyrin G death domain

Summary for 4O6X

• Entry DOI: 10.2210/pdb4o6x/pdb
• Related: 3PSP 3PST
• Descriptor: Ankyrin-3 (2 entities in total)
• Functional Keywords: alpha helix bundle, protein binding, death domain, alpha helix
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton . Isoform 5: Cytoplasm, cytoskeleton : Q12955
• Total number of polymer chains: 2
• Total formula weight: 27642.97

Authors

Liu, Y.,Zhang, Y.,Wang, J.H. (deposition date: 2013-12-24, release date: 2014-10-29, Last modification date: 2023-09-20)

Primary citation

Liu, Y.,Zhang, Y.,Wang, J.H.
Crystal structure of human Ankyrin G death domain.
Proteins, 82:3476-3482, 2014

PubMed Abstract: Ankyrins (Ank) are a ubiquitously expressed family of multifunctional membrane adapter proteins. Ankyrin G (AnkG) is critical for assembling and maintenance of the axon initial segment. Here we present the 2.1 Å crystal structure of human AnkG death domain (hAnkG-DD). The core death domain is composed of six α-helices and three 3₁₀-helices. It forms a hydrophobic pocket on the surface of the molecule. The C-terminal tail of the hAnkG-DD curves back to have the aromatic ring of a phenylalanine residue, Phe100 insert into this pocket, which anchors the flexible tail onto the core domain. Related DDs were selected for structure comparison. The major variations are at the C-terminal region, including the α6 and the long C-terminal extension. The results of size exclusion chromatography and analytical ultracentrifugation suggest that hAnkG-DD exists as monomer in solution. Our work should help for the future investigation of the structure-function of AnkG.

PubMed: 25307106
DOI: 10.1002/prot.24702

Experimental method

X-RAY DIFFRACTION (2.103 Å)