2H0K

Crystal Structure of a Mutant of Rat Annexin A5

Summary for 2H0K

• Entry DOI: 10.2210/pdb2h0k/pdb
• Descriptor: Annexin A5, CALCIUM ION (3 entities in total)
• Functional Keywords: phospholipid membrane binding proteins, blood clotting
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 2
• Total formula weight: 72051.41

Authors

Granier, T.,Langlois D'Estaintot, B.,Gallois, B.,Tessier, B.,Brisson, A. (deposition date: 2006-05-15, release date: 2007-06-19, Last modification date: 2023-08-30)

Primary citation

Bouter, A.,Gounou, C.,Berat, R.,Tan, S.,Gallois, B.,Granier, T.,d'Estaintot, B.L.,Poschl, E.,Brachvogel, B.,Brisson, A.R.
Annexin-A5 assembled into two-dimensional arrays promotes cell membrane repair.
Nat Commun, 2:270-270, 2011

PubMed Abstract: Eukaryotic cells possess a universal repair machinery that ensures rapid resealing of plasma membrane disruptions. Before resealing, the torn membrane is submitted to considerable tension, which functions to expand the disruption. Here we show that annexin-A5 (AnxA5), a protein that self-assembles into two-dimensional (2D) arrays on membranes upon Ca(2+) activation, promotes membrane repair. Compared with wild-type mouse perivascular cells, AnxA5-null cells exhibit a severe membrane repair defect. Membrane repair in AnxA5-null cells is rescued by addition of AnxA5, which binds exclusively to disrupted membrane areas. In contrast, an AnxA5 mutant that lacks the ability of forming 2D arrays is unable to promote membrane repair. We propose that AnxA5 participates in a previously unrecognized step of the membrane repair process: triggered by the local influx of Ca(2+), AnxA5 proteins bind to torn membrane edges and form a 2D array, which prevents wound expansion and promotes membrane resealing.

PubMed: 21468022
DOI: 10.1038/ncomms1270

Experimental method

X-RAY DIFFRACTION (2.76 Å)