1w45
From Proteopedia
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| - | [[Image:1w45.gif|left|200px]]<br /><applet load="1w45" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1w45, resolution 2.51Å" /> | ||
| - | '''THE 2.5 ANGSTROEM STRUCTURE OF THE K16A MUTANT OF ANNEXIN A8, WHICH HAS AN INTACT N-TERMINUS.'''<br /> | ||
| - | == | + | ==The 2.5 Angstroem structure of the K16A mutant of annexin A8, which has an intact N-terminus.== |
| + | <StructureSection load='1w45' size='340' side='right'caption='[[1w45]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1w45]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W45 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]] 2.51Å</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=1w45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w45 OCA], [https://pdbe.org/1w45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w45 RCSB], [https://www.ebi.ac.uk/pdbsum/1w45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w45 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANXA8_HUMAN ANXA8_HUMAN] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | ||
| + | == 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/w4/1w45_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=1w45 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Annexin A8 is a relatively infrequent and poorly studied member of this large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia. We have solved its three-dimensional structure, which includes a moderately long and intact N terminus. The structure is closest to that of annexin A3 and highlights several important regions of inherent flexibility in the annexin molecule. The N terminus resembles that of annexin A3, as it lies along the concave surface of the molecule and inserts partially into the hydrophilic channel in its centre. Since both annexins A3 and A8 are expressed in promyelocytic cells during their differentiation, the similarity in their structures might suggest a functional relationship. | Annexin A8 is a relatively infrequent and poorly studied member of this large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia. We have solved its three-dimensional structure, which includes a moderately long and intact N terminus. The structure is closest to that of annexin A3 and highlights several important regions of inherent flexibility in the annexin molecule. The N terminus resembles that of annexin A3, as it lies along the concave surface of the molecule and inserts partially into the hydrophilic channel in its centre. Since both annexins A3 and A8 are expressed in promyelocytic cells during their differentiation, the similarity in their structures might suggest a functional relationship. | ||
| - | + | The crystal structure of annexin A8 is similar to that of annexin A3.,Rety S, Sopkova-de Oliveira Santos J, Dreyfuss L, Blondeau K, Hofbauerova K, Raguenes-Nicol C, Kerboeuf D, Renouard M, Russo-Marie F, Lewit-Bentley A J Mol Biol. 2005 Feb 4;345(5):1131-9. Epub 2004 Dec 8. PMID:15644210<ref>PMID:15644210</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1w45" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Annexin 3D structures|Annexin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Blondeau K]] | ||
| + | [[Category: Dreyfuss L]] | ||
| + | [[Category: Hofbauerova K]] | ||
| + | [[Category: Lewit-Bentley A]] | ||
| + | [[Category: Raguenes-Nicol C]] | ||
| + | [[Category: Renouard M]] | ||
| + | [[Category: Rety S]] | ||
| + | [[Category: Russo-Marie F]] | ||
| + | [[Category: Sopkova-de Oliveira Santos J]] | ||
Current revision
The 2.5 Angstroem structure of the K16A mutant of annexin A8, which has an intact N-terminus.
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