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 1.80&Aring;" /> '''X-RAY STRUCTURE OF F...)
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[[Image:1hm6.gif|left|200px]]<br /><applet load="1hm6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hm6, resolution 1.80&Aring;" />
 
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'''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1'''<br />
 
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==Overview==
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==X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1==
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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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<StructureSection load='1hm6' size='340' side='right'caption='[[1hm6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hm6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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==
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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>
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1HM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HM6 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11178908 11178908]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1hm6" style="background-color:#fffaf0;"></div>
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[[Category: Sus scrofa]]
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[[Category: Gerke, V.]]
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[[Category: Luecke, H.]]
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[[Category: Rosengarth, A.]]
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[[Category: SO4]]
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[[Category: calcium-free form]]
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[[Category: full-length protein comprising protein core and n-terminal domain]]
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[[Category: phospholipid/ca(2+)-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:38:52 2007''
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==See Also==
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*[[Annexin 3D structures|Annexin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: Gerke V]]
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[[Category: Luecke H]]
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[[Category: Rosengarth A]]

Current revision

X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1

PDB ID 1hm6

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