1wnh

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Current revision (13:32, 13 March 2024) (edit) (undo)
 
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<StructureSection load='1wnh' size='340' side='right'caption='[[1wnh]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='1wnh' size='340' side='right'caption='[[1wnh]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1wnh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WNH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1wnh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WNH FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LXN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1wnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wnh OCA], [http://pdbe.org/1wnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wnh RCSB], [http://www.ebi.ac.uk/pdbsum/1wnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wnh ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wnh OCA], [https://pdbe.org/1wnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wnh RCSB], [https://www.ebi.ac.uk/pdbsum/1wnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wnh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LXN_MOUSE LXN_MOUSE]] Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation.
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[https://www.uniprot.org/uniprot/LXN_MOUSE LXN_MOUSE] Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation.
== 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=1wnh 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=1wnh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Latexin, the only known mammalian carboxypeptidase inhibitor, has no detectable sequence similarity with plant and parasite inhibitors, but it is related to a human putative tumor suppressor protein, TIG1. Latexin is expressed in the developing brain, and we find that it plays a role in inflammation, as it is expressed at high levels and is inducible in macrophages in concert with other protease inhibitors and potential protease targets. The crystal structure of mouse latexin, solved at 1.83 A resolution, shows no structural relationship with other carboxypeptidase inhibitors. Furthermore, despite a lack of detectable sequence duplication, the structure incorporates two topologically analogous domains related by pseudo two-fold symmetry. Surprisingly, these domains share a cystatin fold architecture found in proteins that inhibit cysteine proteases, suggesting an evolutionary and possibly functional relationship. The structure of the tumor suppressor protein TIG1 was modeled, revealing its putative membrane binding surface.
 
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An inflammatory role for the mammalian carboxypeptidase inhibitor latexin: relationship to cystatins and the tumor suppressor TIG1.,Aagaard A, Listwan P, Cowieson N, Huber T, Ravasi T, Wells CA, Flanagan JU, Kellie S, Hume DA, Kobe B, Martin JL Structure. 2005 Feb;13(2):309-17. PMID:15698574<ref>PMID:15698574</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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<div class="pdbe-citations 1wnh" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Aagaard, A]]
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[[Category: Aagaard A]]
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[[Category: Cowieson, N]]
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[[Category: Cowieson N]]
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[[Category: Flanagan, J U]]
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[[Category: Flanagan JU]]
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[[Category: Huber, T]]
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[[Category: Huber T]]
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[[Category: Hume, D A]]
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[[Category: Hume DA]]
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[[Category: Kobe, B]]
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[[Category: Kobe B]]
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[[Category: Listwan, P]]
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[[Category: Listwan P]]
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[[Category: Martin, J L]]
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[[Category: Martin JL]]
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[[Category: Ravasi, T]]
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[[Category: Ravasi T]]
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[[Category: Wells, C A]]
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[[Category: Wells CA]]
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[[Category: Bi-cystatin fold]]
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[[Category: Cis-proline]]
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[[Category: Hydrolase inhibitor]]
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Current revision

Crystal structure of mouse Latexin (tissue carboxypeptidase inhibitor)

PDB ID 1wnh

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