1HM6

X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1

1HM6 の概要

• エントリーDOI: 10.2210/pdb1hm6/pdb
• 分子名称: ANNEXIN 1, SULFATE ION (3 entities in total)
• 機能のキーワード: phospholipid/ca(2+)-binding protein, calcium-free form, full-length protein comprising protein core and n-terminal domain, lipid binding protein, metal
• 由来する生物種: Sus scrofa (pig)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78757.47

構造登録者

Rosengarth, A.,Gerke, V.,Luecke, H. (登録日: 2000-12-04, 公開日: 2001-02-28, 最終更新日: 2024-11-20)

主引用文献

Rosengarth, A.,Gerke, V.,Luecke, H.
X-ray structure of full-length annexin 1 and implications for membrane aggregation.
J.Mol.Biol., 306:489-498, 2001

PubMed 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 A structure shows an alpha-helical N-terminal domain connected to the core domain by a flexible linker. It is surprising that the two alpha-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.

PubMed: 11178908
DOI: 10.1006/jmbi.2000.4423

実験手法

X-RAY DIFFRACTION (1.8 Å)