1hm6
From Proteopedia
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| - | [[Image:1hm6.gif|left|200px]] | + | [[Image:1hm6.gif|left|200px]] |
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| - | '''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1''' | + | {{Structure |
| + | |PDB= 1hm6 |SIZE=350|CAPTION= <scene name='initialview01'>1hm6</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= ANX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa]) | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HM6 is a [ | + | 1HM6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM6 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11178908 11178908] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: phospholipid/ca(2+)-binding protein]] | [[Category: phospholipid/ca(2+)-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:52 2008'' |
Revision as of 09:38, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Gene: | ANX1 (Sus scrofa) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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