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• W2057897974 endingPage "498" @default.
• W2057897974 startingPage "489" @default.
• W2057897974 abstract "Annexins comprise a multigene family of Ca2+ and phospholipid-binding proteins. They consist of a conserved C-terminal or core domain that confers Ca2+-dependent phospholipid binding and an N-terminal domain that is variable in sequence and length and responsible for the specific properties of each annexin. Crystal structures of various annexin core domains have revealed a high degree of similarity. From these and other studies it is evident that the core domain harbors the calcium-binding sites that interact with the phospholipid headgroups. However, no structure has been reported of an annexin with a complete N-terminal domain. We have now solved the crystal structure of such a full-length annexin, annexin 1. Annexin 1 is active in membrane aggregation and its refined 1.8 Å structure shows an α-helical N-terminal domain connected to the core domain by a flexible linker. It is surprising that the two α-helices present in the N-terminal domain of 41 residues interact intimately with the core domain, with the amphipathic helix 2–12 of the N-terminal domain replacing helix D of repeat III of the core. In turn, helix D is unwound into a flap now partially covering the N-terminal helix. Implications for membrane aggregation will be discussed and a model of aggregation based on the structure will be presented." @default.
• W2057897974 created "2016-06-24" @default.
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• W2057897974 creator A5029075284 @default.
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• W2057897974 date "2001-02-01" @default.
• W2057897974 modified "2023-10-03" @default.
• W2057897974 title "X-ray structure of full-length annexin 1 and implications for membrane aggregation11Edited by D. Rees" @default.
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• W2057897974 doi "https://doi.org/10.1006/jmbi.2000.4423" @default.
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