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1qyj

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1qyj.png|left|200px]]
 
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==HISTOASPARTIC PROTEINASE FROM PLASMODIUM FALCIPARUM==
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The line below this paragraph, containing "STRUCTURE_1qyj", creates the "Structure Box" on the page.
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<StructureSection load='1qyj' size='340' side='right'caption='[[1qyj]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYJ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1qyj FirstGlance], [https://www.ebi.ac.uk/pdbsum/1qyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qyj ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1qyj| PDB=1qyj | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The primary structure of the so-called histoaspartic protease from Plasmodium falciparum has a very high percentage of identity and homology with the pepsin-like enzyme plasmepsin II. A homology modeling approach was used to calculate the three-dimensional structure of the enzyme. Molecular dynamics (MD) simulations were applied to find those structural properties of the histoaspartic protease that had a tendency to remain stable during all runs. The results have shown that hydrogen-bonded residues Ser37-His34-Asp214 are arranged without any strain, in a manner that resembles the active site of a serine protease, while Ser38 and Asn39 take up positions appropriate to formation of an oxyanion hole. Although there are several important differences between the enzyme and plasmepsin II, all of the structural features associated with a typical pepsin-like aspartic protease are present in the final model of the histoaspartic protease. A possibility that this enzyme may function as a serine protease is discussed.
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===HISTOASPARTIC PROTEINASE FROM PLASMODIUM FALCIPARUM===
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Is histoaspartic protease a serine protease with a pepsin-like fold?,Andreeva N, Bogdanovich P, Kashparov I, Popov M, Stengach M Proteins. 2004 May 15;55(3):705-10. PMID:15103632<ref>PMID:15103632</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15103632}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qyj" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15103632 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15103632}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYJ OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:15103632</ref><references group="xtra"/>
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[[Category: Andreeva, N S]]
[[Category: Andreeva, N S]]
[[Category: Bogdanovitch, P M]]
[[Category: Bogdanovitch, P M]]
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[[Category: Popov, M E]]
[[Category: Popov, M E]]
[[Category: Stengach, M A]]
[[Category: Stengach, M A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 07:25:24 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

HISTOASPARTIC PROTEINASE FROM PLASMODIUM FALCIPARUM

PDB ID 1qyj

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