1hm6
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(New page: 200px<br /><applet load="1hm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hm6, resolution 1.80Å" /> '''X-RAY STRUCTURE OF F...)
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Revision as of 14:31, 20 November 2007
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X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1
Overview
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.
About this Structure
1HM6 is a Single protein structure of sequence from Sus scrofa with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
X-ray structure of full-length annexin 1 and implications for membrane aggregation., Rosengarth A, Gerke V, Luecke H, J Mol Biol. 2001 Feb 23;306(3):489-98. PMID:11178908
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