1hm6: Difference between revisions

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[[Image:1hm6.gif|left|200px]]
{{Seed}}
[[Image:1hm6.png|left|200px]]


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{{STRUCTURE_1hm6|  PDB=1hm6  |  SCENE=  }}  
{{STRUCTURE_1hm6|  PDB=1hm6  |  SCENE=  }}  


'''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1'''
===X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Calcium-free form]]
[[Category: Calcium-free form]]
[[Category: Full-length protein comprising protein core and n-terminal domain]]
[[Category: Full-length protein comprising protein core and n-terminal domain]]
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