2a4i

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:2a4i.png|left|200px]]
 
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==HOMOLOGY MODEL OF VIMELYSIN==
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The line below this paragraph, containing "STRUCTURE_2a4i", creates the "Structure Box" on the page.
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<StructureSection load='2a4i' size='340' side='right'caption='[[2a4i]]' 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=2A4I 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=2a4i FirstGlance], [https://www.ebi.ac.uk/pdbsum/2a4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a4i ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2a4i| PDB=2a4i | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vimelysin is a metalloproteinase with high activity at low temperature and an unusual resistance to organic solvents. Substrate specificities of vimelysin and thermolysin were examined using FRETS-libraries, revealing a significant difference at the P3' position: vimelysin preferred acidic amino acid residues, whereas thermolysin preferred basic residues. Homology modeling of vimelysin suggests that oppositely charged residues in the S3' subsites (R215 in vimelysin and D213 in thermolysin) may be responsible for this specificity difference. This hypothesis was confirmed by examining the R215D mutant of vimelysin, which showed a substrate specificity profile intermediate between thermolysin and vimelysin.
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===HOMOLOGY MODEL OF VIMELYSIN===
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Exploring the subsite-structure of vimelysin and thermolysin using FRETS-libraries.,Oda K, Takahashi T, Takada K, Tsunemi M, Ng KK, Hiraga K, Harada S FEBS Lett. 2005 Sep 12;579(22):5013-8. PMID:16139276<ref>PMID:16139276</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_16139276}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2a4i" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16139276 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16139276}}
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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=2A4I OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:16139276</ref><references group="xtra"/>
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[[Category: Harada, S]]
[[Category: Harada, S]]
[[Category: Hiraga, K]]
[[Category: Hiraga, K]]
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[[Category: Takahashi, T]]
[[Category: Takahashi, T]]
[[Category: Tsunemi, M]]
[[Category: Tsunemi, M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:49:51 2010''
 

Current revision

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

HOMOLOGY MODEL OF VIMELYSIN

PDB ID 2a4i

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OCA

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