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[[Image:1hm6.gif|left|200px]]
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{{STRUCTURE_1hm6|  PDB=1hm6  |  SCENE=  }}
'''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1'''


==X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1==
<StructureSection load='1hm6' size='340' side='right'caption='[[1hm6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hm6]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HM6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hm6 OCA], [https://pdbe.org/1hm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hm6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ANXA1_PIG ANXA1_PIG] Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hm6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hm6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:11178908</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1hm6" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Annexin 3D structures|Annexin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Gerke, V.]]
[[Category: Gerke V]]
[[Category: Luecke, H.]]
[[Category: Luecke H]]
[[Category: Rosengarth, A.]]
[[Category: Rosengarth A]]
[[Category: Calcium-free form]]
[[Category: Full-length protein comprising protein core and n-terminal domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:00:23 2008''
Retrieved from "https://proteopedia.org/1hm6"