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1mzd

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crystal structure of human pro-granzyme K

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Retrieved from "http://52.214.119.220/wiki/index.php/1mzd"

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-[[Image:1mzd.gif|left|200px]]<br />
-<applet load="1mzd" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1mzd, resolution 2.9&Aring;" />
-'''crystal structure of human pro-granzyme K'''<br />
-==Overview==
+==crystal structure of human pro-granzyme K==
-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.
+<StructureSection load='1mzd' size='340' side='right'caption='[[1mzd]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GRAK_HUMAN GRAK_HUMAN]
+== 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/mz/1mzd_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=1mzd ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-MZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MZD OCA].
+*[[Granzyme|Granzyme]]
+__TOC__
-==Reference==
+</StructureSection>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12384499 12384499]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[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: s1 family]]
-[[Category: serine protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:16:11 2007''

1mzd

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Current revision

crystal structure of human pro-granzyme K

Structural highlights

Function

Evolutionary Conservation

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