| First Author | Dempsey BR | Year | 2012 |
| Journal | Structure | Volume | 20 |
| Issue | 10 | Pages | 1737-45 |
| PubMed ID | 22940583 | Mgi Jnum | J:320055 |
| Mgi Id | MGI:6867287 | Doi | 10.1016/j.str.2012.08.004 |
| Citation | Dempsey BR, et al. (2012) Structure of an asymmetric ternary protein complex provides insight for membrane interaction. Structure 20(10):1737-45 |
| abstractText | Plasma membrane repair involves the coordinated effort of proteins and the inner phospholipid surface to mend the rupture and return the cell back to homeostasis. Here, we present the three-dimensional structure of a multiprotein complex that includes S100A10, annexin A2, and AHNAK, which along with dysferlin, functions in muscle and cardiac tissue repair. The 3.5 A resolution X-ray structure shows that a single region from the AHNAK C terminus is recruited by an S100A10-annexin A2 heterotetramer, forming an asymmetric ternary complex. The AHNAK peptide adopts a coil conformation that arches across the heterotetramer contacting both annexin A2 and S100A10 protomers with tight affinity ( approximately 30 nM) and establishing a structural rationale whereby both S100A10 and annexin proteins are needed in AHNAK recruitment. The structure evokes a model whereby AHNAK is targeted to the membrane surface through sandwiching of the binding region between the S100A10/annexin A2 complex and the phospholipid membrane. |
