2zrs: Difference between revisions
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==Crystal structure of Ca2+-bound form of des3-23ALG-2== | ==Crystal structure of Ca2+-bound form of des3-23ALG-2== | ||
<StructureSection load='2zrs' size='340' side='right' caption='[[2zrs]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='2zrs' size='340' side='right' caption='[[2zrs]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zn9|2zn9]], [[2znd|2znd]], [[2zne|2zne]], [[2zrt|2zrt]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zn9|2zn9]], [[2znd|2znd]], [[2zne|2zne]], [[2zrt|2zrt]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDCD6, ALG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDCD6, ALG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zrs OCA], [http://pdbe.org/2zrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zrs RCSB], [http://www.ebi.ac.uk/pdbsum/2zrs PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zrs OCA], [http://pdbe.org/2zrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zrs RCSB], [http://www.ebi.ac.uk/pdbsum/2zrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zrs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2zrs" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2zrs" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Wakatsuki, S]] | [[Category: Wakatsuki, S]] | ||
[[Category: Apoptosis]] | [[Category: Apoptosis]] | ||
[[Category: Calcium]] | |||
[[Category: Calcium-binding protein]] | [[Category: Calcium-binding protein]] | ||
[[Category: Endoplasmic reticulum]] | [[Category: Endoplasmic reticulum]] | ||
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[[Category: Nucleus]] | [[Category: Nucleus]] | ||
[[Category: Penta-ef-hand protein]] | [[Category: Penta-ef-hand protein]] | ||
[[Category: Polymorphism]] | |||
Revision as of 15:25, 12 October 2017
Crystal structure of Ca2+-bound form of des3-23ALG-2Crystal structure of Ca2+-bound form of des3-23ALG-2
Structural highlights
Function[PDCD6_HUMAN] Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca(2+)-regulated signals along the death pathway (By similarity). Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity.[1] [2] 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 PubMedALG-2 (apoptosis-linked gene 2) is an apoptosis-linked calcium-binding protein with five EF-hand motifs in the C-terminal region. N-terminally truncated ALG-2 (des3-23ALG-2) was crystallized by the vapour-diffusion method in buffer consisting of either 50 mM MES pH 6.5, 12.5%(v/v) 2-propanol and 150 mM calcium acetate or 100 mM MES pH 6.0, 15%(v/v) ethanol and 200 mM zinc acetate. Crystals of the Ca(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 54.8, b = 154.4, c = 237.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.1 A resolution. Crystals of the Zn(2+)-bound form belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 52.8, b = 147.5, c = 230.7 A, alpha = beta = gamma = 90 degrees , and diffracted to 3.3 A resolution. The structures of the Ca(2+)-bound form and the Zn(2+)-bound form were solved by the molecular-replacement method. Although both crystals contained eight ALG-2 molecules per asymmetric unit, the metal-ion locations and octameric arrangements were found to be significantly different. Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2.,Suzuki H, Kawasaki M, Kakiuchi T, Shibata H, Wakatsuki S, Maki M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt, 11):974-7. Epub 2008 Oct 31. PMID:18997320[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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