3h6r: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3h6r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clitocybe_nebularis Clitocybe nebularis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H6R FirstGlance]. <br>
<table><tr><td colspan='2'>[[3h6r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clitocybe_nebularis Clitocybe nebularis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H6R FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3h6q|3h6q]], [[3h6s|3h6s]]</div></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]] 1.948&#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=3h6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6r OCA], [https://pdbe.org/3h6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h6r RCSB], [https://www.ebi.ac.uk/pdbsum/3h6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h6r ProSAT]</span></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=3h6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6r OCA], [https://pdbe.org/3h6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h6r RCSB], [https://www.ebi.ac.uk/pdbsum/3h6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h6r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CLIT2_CLINE CLIT2_CLINE]] Binds and inhibits cysteine proteinases. Inhibits most strongly papain and cathepsin L, more weakly bromelain and cathepsin B while it is completely ineffective against cathepsin H.  
[https://www.uniprot.org/uniprot/CLIT2_CLINE CLIT2_CLINE] Binds and inhibits cysteine proteinases. Inhibits most strongly papain and cathepsin L, more weakly bromelain and cathepsin B while it is completely ineffective against cathepsin H.
== 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=3h6r 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=3h6r ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycocypins, clitocypins and macrocypins, are cysteine protease inhibitors isolated from the mushrooms Clitocybe nebularis and Macrolepiota procera. Lack of sequence homology to other families of protease inhibitors suggested that mycocypins inhibit their target cysteine protease by a unique mechanism and that a novel fold may be found. The crystal structures of the complex of clitocypin with the papain-like cysteine protease cathepsin V and of macrocypin and clitocypin alone have revealed yet another motif of binding to papain like-cysteine proteases, which in a yet unrevealed way occludes the catalytic residue. The binding is associated with a peptide-bond flip of glycine that occurs before or concurrently with the inhibitor docking. Mycocypins possess a beta-trefoil fold, the hallmark of Kunitz-type inhibitors. It is a tree-like structure with two loops in the root region, a stem comprising a six-stranded beta-barrel, and two layers of loops (6 + 3) in the crown region. The two loops that bind to cysteine cathepsins belong to the lower layer of the crown loops, whereas a single loop from the crown region can inhibit trypsin or asparaginyl endopeptidase, as demonstrated by site-directed mutagenesis. These loops present a versatile surface with the potential to bind to additional classes of proteases. When appropriately engineered, they could provide the basis for possible exploitation in crop protection.
Versatile loops in mycocypins inhibit three protease families.,Renko M, Sabotic J, Mihelic M, Brzin J, Kos J, Turk D J Biol Chem. 2010 Jan 1;285(1):308-16. Epub 2009 Oct 21. PMID:19846555<ref>PMID:19846555</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3h6r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clitocybe nebularis]]
[[Category: Clitocybe nebularis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Brzin, J]]
[[Category: Brzin J]]
[[Category: Renko, M]]
[[Category: Renko M]]
[[Category: Sabotic, J]]
[[Category: Sabotic J]]
[[Category: Turk, D]]
[[Category: Turk D]]
[[Category: Beta trefoil]]
[[Category: Clitocypin]]
[[Category: Cysteine proteinase inhibitor]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Kunitz inhibitor]]

Latest revision as of 09:58, 21 February 2024

Clitocypin, a beta-trefoil cysteine protease inhibitor

3h6r, resolution 1.95Å

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