1mzd: Difference between revisions

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<StructureSection load='1mzd' size='340' side='right'caption='[[1mzd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1mzd' size='340' side='right'caption='[[1mzd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZD FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mzd]] 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=1MZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZD FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mza|1mza]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=1mzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzd OCA], [https://pdbe.org/1mzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzd RCSB], [https://www.ebi.ac.uk/pdbsum/1mzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzd ProSAT]</span></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=1mzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzd OCA], [https://pdbe.org/1mzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzd RCSB], [https://www.ebi.ac.uk/pdbsum/1mzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GRAK_HUMAN GRAK_HUMAN]
== 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=1mzd 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=1mzd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Granzyme K (GzmK) belongs to a family of trypsin-like serine proteases localized in electron dense cytoplasmic granules of activated natural killer and cytotoxic T-cells. Like the related granzymes A and B, GzmK can trigger DNA fragmentation and is involved in apoptosis. We expressed the Ser(195) --&gt; Ala variant of human pro-GzmK in Escherichia coli, crystallized it, and determined its 2.2-A x-ray crystal structure. Pro-GzmK possesses a surprisingly rigid structure, which is most similar to activated serine proteases, in particular complement factor D, and not their proforms. The N-terminal peptide Met(14)-Ile(17) projects freely into solution and can be readily approached by cathepsin C, the natural convertase of pro-granzymes. The pre-shaped S1 pocket is occupied by the ion paired residues Lys(188B)-Asp(194) and is hence not available for proper substrate binding. The Ser(214)-Cys(220) segment, which normally provides a template for substrate binding, bulges out of the active site and is distorted. With analogy to complement factor D, we suggest that this strand will maintain its non-productive conformation in mature GzmK, mainly due to the unusual residues Gly(215), Glu(219), and Val(94). We hypothesize that GzmK is proteolytically active only toward specific, as yet unidentified substrates, which upon approach transiently induce a functional active-site conformation.
The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features.,Hink-Schauer C, Estebanez-Perpina E, Wilharm E, Fuentes-Prior P, Klinkert W, Bode W, Jenne DE J Biol Chem. 2002 Dec 27;277(52):50923-33. Epub 2002 Oct 15. PMID:12384499<ref>PMID:12384499</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mzd" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Granzyme|Granzyme]]
*[[Granzyme|Granzyme]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bode, W]]
[[Category: Bode W]]
[[Category: Estebanez-Perpina, E]]
[[Category: Estebanez-Perpina E]]
[[Category: Fuentes-Prior, P]]
[[Category: Fuentes-Prior P]]
[[Category: Hink-Schauer, C]]
[[Category: Hink-Schauer C]]
[[Category: Jenne, D E]]
[[Category: Jenne DE]]
[[Category: Klinkert, W]]
[[Category: Klinkert W]]
[[Category: Wilharm, E]]
[[Category: Wilharm E]]
[[Category: Apoptosis]]
[[Category: Granzyme]]
[[Category: Hydrolase]]
[[Category: S1 family]]
[[Category: Serine protease]]

Revision as of 06:08, 3 April 2024

crystal structure of human pro-granzyme K

1mzd, resolution 2.90Å

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