1f1j: Difference between revisions

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New page: left|200px<br /> <applet load="1f1j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f1j, resolution 2.35Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1f1j.gif|left|200px]]<br />
<applet load="1f1j" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f1j, resolution 2.35&Aring;" />
'''CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO'''<br />


==Overview==
==CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO==
BACKGROUND: Peptide inhibitors of caspases have helped define the role of, these cysteine proteases in biology. Structural and biochemical, characterization of the caspase enzymes may contribute to the development, of new drugs for the treatment of caspase-mediated inflammation and, apoptosis. RESULTS: The crystal structure of the previously unpublished, caspase-7 (Csp7; 2.35 A) bound to the reversible tetrapeptide aldehyde, inhibitor acetyl-Asp-Glu-Val-Asp-CHO is compared with crystal structures, of caspases-1 (2.3 A), -3 (2.2 A), and -8 (2.65 A) bound to the same, inhibitor. Csp7 is a close homolog of caspase-3 (Csp3), and these two, caspases possess some quarternary structural characteristics that support, their unique role among the caspase family. However, although Csp3 and, Csp7 are quite similar overall, they were found to have a significantly, different substitution pattern of amino acids in and around the S4-binding, site. CONCLUSIONS: These structures span all three caspase subgroups, and, provide a basis for inferring substrate and inhibitor binding, as well as, selectivity for the entire caspase family. This information will influence, the design of selective caspase inhibitors to further elucidate the role, of caspases in biology and hopefully lead to the design of therapeutic, agents to treat caspase-mediated diseases, such as rheumatoid arthritis, certain neurogenerative diseases and stroke.
<StructureSection load='1f1j' size='340' side='right'caption='[[1f1j]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f1j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The August 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Caspases''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_8 10.2210/rcsb_pdb/mom_2004_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1J 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ASJ:(3S)-3-AMINO-4-HYDROXYBUTANOIC+ACID'>ASJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1f1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1j OCA], [https://pdbe.org/1f1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1j RCSB], [https://www.ebi.ac.uk/pdbsum/1f1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CASP7_HUMAN CASP7_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.
== 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/f1/1f1j_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=1f1j ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F1J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1F1J with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb56_1.html Caspases]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F1J OCA].
*[[Caspase 3D structures|Caspase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity., Wei Y, Fox T, Chambers SP, Sintchak J, Coll JT, Golec JM, Swenson L, Wilson KP, Charifson PS, Chem Biol. 2000 Jun;7(6):423-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10873833 10873833]
[[Category: Caspases]]
[[Category: Caspases]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Charifson, P.S.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Wei, Y.]]
[[Category: Charifson PS]]
[[Category: ACE]]
[[Category: Wei Y]]
[[Category: SO4]]
[[Category: caspase-7]]
[[Category: cysteine protease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:48:28 2007''

Latest revision as of 13:09, 20 March 2024

CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHOCRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO

Structural highlights

1f1j is a 4 chain structure with sequence from Homo sapiens. The August 2004 RCSB PDB Molecule of the Month feature on Caspases by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CASP7_HUMAN Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.

Evolutionary Conservation

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

See Also

1f1j, resolution 2.35Å

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