6TU2

Crystal structure of rat annexin A11

Summary for 6TU2

• Entry DOI: 10.2210/pdb6tu2/pdb
• Descriptor: Annexin, CALCIUM ION (3 entities in total)
• Functional Keywords: annexin, calcium, core domain, lipid binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 3
• Total formula weight: 111065.32

Authors

Raasakka, A.,Lillebostad, P.,Vedeler, A.,Kursula, P. (deposition date: 2020-01-01, release date: 2020-05-06, Last modification date: 2024-01-24)

Primary citation

Lillebostad, P.A.G.,Raasakka, A.,Hjellbrekke, S.J.,Patil, S.,Rostbo, T.,Hollas, H.,Sakya, S.A.,Szigetvari, P.D.,Vedeler, A.,Kursula, P.
Structure of the ALS Mutation Target Annexin A11 Reveals a Stabilising N-Terminal Segment.
Biomolecules, 10:-, 2020

PubMed Abstract: The functions of the annexin family of proteins involve binding to Ca, lipid membranes, other proteins, and RNA, and the annexins share a common folded core structure at the C terminus. Annexin A11 (AnxA11) has a long N-terminal region, which is predicted to be disordered, binds RNA, and forms membraneless organelles involved in neuronal transport. Mutations in AnxA11 have been linked to amyotrophic lateral sclerosis (ALS). We studied the structure and stability of AnxA11 and identified a short stabilising segment in the N-terminal end of the folded core, which links domains I and IV. The crystal structure of the AnxA11 core highlights main-chain hydrogen bonding interactions formed through this bridging segment, which are likely conserved in most annexins. The structure was also used to study the currently known ALS mutations in AnxA11. Three of these mutations correspond to buried Arg residues highly conserved in the annexin family, indicating central roles in annexin folding. The structural data provide starting points for detailed structure-function studies of both full-length AnxA11 and the disease variants being identified in ALS.

PubMed: 32344647
DOI: 10.3390/biom10040660

Experimental method

X-RAY DIFFRACTION (2.3 Å)