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New page: left|200px<br /> <applet load="1w3w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w3w, resolution 1.99Å" /> '''THE 2.1 ANGSTROEM R... |
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== | ==The 2.1 Angstroem resolution structure of annexin A8== | ||
Annexin A8 is a relatively infrequent and poorly studied member of this | <StructureSection load='1w3w' size='340' side='right'caption='[[1w3w]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1w3w]] is a 1 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=1W3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W3W 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]] 1.99Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1w3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3w OCA], [https://pdbe.org/1w3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w3w RCSB], [https://www.ebi.ac.uk/pdbsum/1w3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w3w 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/w3/1w3w_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=1w3w 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1w3w" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Annexin 3D structures|Annexin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Lewit-Bentley | [[Category: Lewit-Bentley A]] | ||
[[Category: Renouard | [[Category: Renouard M]] | ||
[[Category: Rety | [[Category: Rety S]] | ||
[[Category: | [[Category: Sopkova-De Oliveira Santos J]] | ||
Latest revision as of 11:53, 6 November 2024
The 2.1 Angstroem resolution structure of annexin A8The 2.1 Angstroem resolution structure of annexin A8
Structural highlights
FunctionANXA8_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAnnexin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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