5Y4F

Crystal Structure of AnkB Ankyrin Repeats R13-24 in complex with autoinhibition segment AI-c

Summary for 5Y4F

• Entry DOI: 10.2210/pdb5y4f/pdb
• Descriptor: Ankyrin-2, CALCIUM ION, ACETATE ION, ... (4 entities in total)
• Functional Keywords: ank repeat, protein-protein interaction, structural protein, auto-inhibition, protein binding
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytoskeleton : Q01484
• Total number of polymer chains: 2
• Total formula weight: 94812.58

Authors

Chen, K.,Li, J.,Wang, C.,Wei, Z.,Zhang, M. (deposition date: 2017-08-03, release date: 2017-09-13, Last modification date: 2023-11-22)

Primary citation

Chen, K.,Li, J.,Wang, C.,Wei, Z.,Zhang, M.
Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.
Elife, 6:-, 2017

PubMed Abstract: Ankyrins together with their spectrin partners are the master organizers of micron-scale membrane domains in diverse tissues. The 24 ankyrin (ANK) repeats of ankyrins bind to numerous membrane proteins, linking them to spectrin-based cytoskeletons at specific membrane microdomains. The accessibility of the target binding groove of ANK repeats must be regulated to achieve spatially defined functions of ankyrins/target complexes in different tissues, though little is known in this regard. Here we systemically investigated the autoinhibition mechanism of ankyrin-B/G by combined biochemical, biophysical and structural biology approaches. We discovered that the entire ANK repeats are inhibited by combinatorial and quasi-independent bindings of multiple disordered segments located in the ankyrin-B/G linkers and tails, suggesting a mechanistic basis for differential regulations of membrane target bindings by ankyrins. In addition to elucidating the autoinhibition mechanisms of ankyrins, our study may also shed light on regulations on target bindings by other long repeat-containing proteins.

PubMed: 28841137
DOI: 10.7554/eLife.29150

Experimental method

X-RAY DIFFRACTION (1.953 Å)