1df0: Difference between revisions

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[[Image:1df0.gif|left|200px]]


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==Crystal structure of M-Calpain==
The line below this paragraph, containing "STRUCTURE_1df0", creates the "Structure Box" on the page.
<StructureSection load='1df0' size='340' side='right'caption='[[1df0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1df0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DF0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=1df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df0 OCA], [https://pdbe.org/1df0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1df0 RCSB], [https://www.ebi.ac.uk/pdbsum/1df0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1df0 ProSAT]</span></td></tr>
{{STRUCTURE_1df0| PDB=1df0 |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAN2_RAT CAN2_RAT] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
== 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/df/1df0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1df0 ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF M-CALPAIN'''
==See Also==
 
*[[Calpain 3D structures|Calpain 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The combination of thiol protease activity and calmodulin-like EF-hands is a feature unique to the calpains. The regulatory mechanisms governing calpain activity are complex, and the nature of the Ca(2+)-induced switch between inactive and active forms has remained elusive in the absence of structural information. We describe here the 2.6 A crystal structure of m-calpain in the Ca(2+)-free form, which illustrates the structural basis for the inactivity of calpain in the absence of Ca(2+). It also reveals an unusual thiol protease fold, which is associated with Ca(2+)-binding domains through heterodimerization and a C(2)-like beta-sandwich domain. Strikingly, the structure shows that the catalytic triad is not assembled, indicating that Ca(2+)-binding must induce conformational changes that re-orient the protease domains to form a functional active site. The alpha-helical N-terminal anchor of the catalytic subunit does not occupy the active site but inhibits its assembly and regulates Ca(2+)-sensitivity through association with the regulatory subunit. This Ca(2+)-dependent activation mechanism is clearly distinct from those of classical proteases.
[[Category: Large Structures]]
 
==About this Structure==
1DF0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA].
 
==Reference==
Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation., Hosfield CM, Elce JS, Davies PL, Jia Z, EMBO J. 1999 Dec 15;18(24):6880-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10601010 10601010]
[[Category: Hydrolase]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Davies, P L.]]
[[Category: Davies PL]]
[[Category: Elce, J S.]]
[[Category: Elce JS]]
[[Category: Hosfield, C M.]]
[[Category: Hosfield CM]]
[[Category: Jia, Z.]]
[[Category: Jia Z]]
[[Category: C2 domain]]
[[Category: Calcium]]
[[Category: Calmodulin]]
[[Category: Calpain]]
[[Category: Catalytic triad]]
[[Category: Cysteine protease]]
[[Category: Papain]]
[[Category: Protease]]
[[Category: Zymogen]]
[[Category: Zymogen activation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:46:38 2008''

Latest revision as of 09:52, 7 February 2024

Crystal structure of M-CalpainCrystal structure of M-Calpain

Structural highlights

1df0 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAN2_RAT Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1df0, resolution 2.60Å

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