1egp: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1egp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGP FirstGlance]. <br>
<table><tr><td colspan='2'>[[1egp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGP FirstGlance]. <br>
</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=1egp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egp OCA], [https://pdbe.org/1egp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egp RCSB], [https://www.ebi.ac.uk/pdbsum/1egp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egp ProSAT]</span></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&#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=1egp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egp OCA], [https://pdbe.org/1egp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egp RCSB], [https://www.ebi.ac.uk/pdbsum/1egp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.  
[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME] Inhibits both elastase and cathepsin G.
== 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=1egp 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=1egp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The inhibition of serine proteinases by both synthetic and natural inhibitors has been widely studied. Eglin c is a small thermostable protein isolated from the leech, Hirudo medicinalis. Eglin c is a potent serine proteinase inhibitor. The three-dimensional structure of native eglin and of its complexes with a number of proteinases are known. We here describe the crystal structure of hydrolysed eglin not bound to a proteinase. The body of the eglin has a conformation remarkably similar to that in the known complexes with proteinases. However, the peptide chain has been cut at the 'scissile' bond between residues 45 and 46, presumed to result from the presence of subtilisin DY in the crystallisation sample. The residues usually making up the inhibiting loop of eglin take up a quite different conformation in the nicked inhibitor leading to stabilising contacts between neighbouring molecules in the crystal. The structure was solved by molecular replacement techniques and refined to a final R-factor of 14.5%.
Structure of the proteinase inhibitor eglin c with hydrolysed reactive centre at 2.0 A resolution.,Betzel C, Dauter Z, Genov N, Lamzin V, Navaza J, Schnebli HP, Visanji M, Wilson KS FEBS Lett. 1993 Feb 15;317(3):185-8. PMID:8425603<ref>PMID:8425603</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1egp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Eglin|Eglin]]
*[[Eglin|Eglin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Betzel, C]]
[[Category: Betzel C]]
[[Category: Dauter, Z]]
[[Category: Dauter Z]]
[[Category: Lamzin, V]]
[[Category: Lamzin V]]
[[Category: Wilson, K S]]
[[Category: Wilson KS]]
[[Category: Proteinase inhibitor]]

Latest revision as of 10:02, 7 February 2024

PROTEINASE INHIBITOR EGLIN C WITH HYDROLYSED REACTIVE CENTERPROTEINASE INHIBITOR EGLIN C WITH HYDROLYSED REACTIVE CENTER

Structural highlights

1egp is a 2 chain structure with sequence from Hirudo medicinalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ICIC_HIRME Inhibits both elastase and cathepsin G.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1egp, resolution 2.00Å

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OCA
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