1nx0
From Proteopedia
(Difference between revisions)
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<StructureSection load='1nx0' size='340' side='right'caption='[[1nx0]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1nx0' size='340' side='right'caption='[[1nx0]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1nx0]] is a 5 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1nx0]] is a 5 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=1NX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NX0 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
- | <tr id=' | + | <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=1nx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nx0 OCA], [https://pdbe.org/1nx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1nx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nx0 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/CPNS1_PIG CPNS1_PIG] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1nx0 ConSurf]. | </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=1nx0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The Ca(2+)-dependent cysteine protease calpain along with its endogenous inhibitor calpastatin is widely distributed. The interactions between calpain and calpastatin have been studied to better understand the nature of calpain inhibition by calpastatin, which can aid the design of small molecule inhibitors to calpain. Here we present the crystal structure of a complex between a calpastatin peptide and the calcium-binding domain VI of calpain. DIC19 is a 19 residue peptide, which corresponds to one of the three interacting domains of calpastatin, which is known to interact with domain VI of calpain. We present two crystal structures of DIC19 bound to domain VI of calpain, determined by molecular replacement methods to 2.5A and 2.2A resolution. In the process of crystallizing the inhibitor complex, a new native crystal form was identified which had the homodimer 2-fold axis along a crystallographic axis as opposed to the previously observed dimer in the asymmetric unit. The crystal structures of the native domain VI and its inhibitor PD150606 (3-(4-iodophenyl)-2-mercapto-(Z)-2-propenoic acid) complex were determined with the help of molecular replacement methods to 2.0A and 2.3A resolution, respectively. In addition, we built a homology model for the complex between domain IV and DIA19 peptide of calpastatin. Finally, we present a model for the calpastatin-inhibited calpain. | ||
- | |||
- | A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor.,Todd B, Moore D, Deivanayagam CC, Lin GD, Chattopadhyay D, Maki M, Wang KK, Narayana SV J Mol Biol. 2003 Apr 18;328(1):131-46. PMID:12684003<ref>PMID:12684003</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1nx0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Calpain 3D structures|Calpain 3D structures]] | *[[Calpain 3D structures|Calpain 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Sus scrofa]] |
- | [[Category: Chattopadhyay | + | [[Category: Chattopadhyay D]] |
- | [[Category: Deivanayagam | + | [[Category: Deivanayagam CCS]] |
- | [[Category: Lin | + | [[Category: Lin G-D]] |
- | [[Category: Maki | + | [[Category: Maki M]] |
- | [[Category: Moore | + | [[Category: Moore D]] |
- | [[Category: Narayana | + | [[Category: Narayana SVL]] |
- | [[Category: Todd | + | [[Category: Todd B]] |
- | [[Category: Wang | + | [[Category: Wang KKW]] |
- | + | ||
- | + |
Current revision
Structure of Calpain Domain 6 in Complex with Calpastatin DIC
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Categories: Large Structures | Sus scrofa | Chattopadhyay D | Deivanayagam CCS | Lin G-D | Maki M | Moore D | Narayana SVL | Todd B | Wang KKW