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[[Image:1avf.gif|left|200px]]
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{{STRUCTURE_1avf|  PDB=1avf  |  SCENE=  }}
'''ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH'''


==ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH==
<StructureSection load='1avf' size='340' side='right'caption='[[1avf]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1avf]] is a 4 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=1AVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVF 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]] 2.36&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=1avf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avf OCA], [https://pdbe.org/1avf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1avf RCSB], [https://www.ebi.ac.uk/pdbsum/1avf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PEPC_HUMAN PEPC_HUMAN] Hydrolyzes a variety of proteins.
== 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/av/1avf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1avf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of an activation intermediate of human gastricsin has been determined at 2.4 A resolution. The human digestive enzyme gastricsin (pepsin C) is an aspartic proteinase that is synthesized as the inactive precursor (zymogen) progastricsin (pepsinogen C or hPGC). In the zymogen, a positively-charged N-terminal prosegment of 43 residues (Ala 1p-Leu 43p; the suffix 'p' refers to the prosegment) sterically prevents the approach of a substrate to the active site. Zymogen conversion occurs in an autocatalytic and stepwise fashion at low pH through the formation of intermediates. The structure of the non-covalent complex of a partially-cleaved peptide of the prosegment (Ala 1p-Phe 26p) with mature gastricsin (Ser 1-Ala 329) suggests an activation pathway that may be common to all gastric aspartic proteinases.


==Overview==
Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin.,Khan AR, Cherney MM, Tarasova NI, James MN Nat Struct Biol. 1997 Dec;4(12):1010-5. PMID:9406551<ref>PMID:9406551</ref>
The crystal structure of an activation intermediate of human gastricsin has been determined at 2.4 A resolution. The human digestive enzyme gastricsin (pepsin C) is an aspartic proteinase that is synthesized as the inactive precursor (zymogen) progastricsin (pepsinogen C or hPGC). In the zymogen, a positively-charged N-terminal prosegment of 43 residues (Ala 1p-Leu 43p; the suffix 'p' refers to the prosegment) sterically prevents the approach of a substrate to the active site. Zymogen conversion occurs in an autocatalytic and stepwise fashion at low pH through the formation of intermediates. The structure of the non-covalent complex of a partially-cleaved peptide of the prosegment (Ala 1p-Phe 26p) with mature gastricsin (Ser 1-Ala 329) suggests an activation pathway that may be common to all gastric aspartic proteinases.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1AVF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVF OCA].
</div>
<div class="pdbe-citations 1avf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin., Khan AR, Cherney MM, Tarasova NI, James MN, Nat Struct Biol. 1997 Dec;4(12):1010-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9406551 9406551]
*[[Pepsin|Pepsin]]
[[Category: Gastricsin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Cherney, M M.]]
[[Category: Cherney MM]]
[[Category: James, M N.G.]]
[[Category: James MNG]]
[[Category: Khan, A R.]]
[[Category: Khan AR]]
[[Category: Tarasova, N I.]]
[[Category: Tarasova NI]]
[[Category: Acid]]
[[Category: Activation]]
[[Category: Aspartic proteinase]]
[[Category: Aspartyl protease]]
[[Category: Gastricsin]]
[[Category: Intermediate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:44:28 2008''

Latest revision as of 06:23, 30 October 2024

ACTIVATION INTERMEDIATE 2 OF HUMAN GASTRICSIN FROM HUMAN STOMACH

1avf, resolution 2.36Å

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