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[[Image:1glo.jpg|left|200px]]
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{{STRUCTURE_1glo|  PDB=1glo  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF CYS25SER MUTANT OF HUMAN CATHEPSIN S'''


==Crystal Structure of Cys25Ser mutant of human cathepsin S==
<StructureSection load='1glo' size='340' side='right'caption='[[1glo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1glo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=1glo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glo OCA], [https://pdbe.org/1glo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glo RCSB], [https://www.ebi.ac.uk/pdbsum/1glo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1glo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1glo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cathepsin S (EC 3.4.22.27), a cysteine proteinase of the papain superfamily, plays a critical role in the generation of a major histocompatibility complex (MHC) class II restricted T-cell response by antigen-presenting cells. Therefore, selective inhibition of this enzyme may be useful in modulating class II restricted T-cell responses in immune-related disorders such as rheumatoid arthritis, multiple sclerosis and extrinsic asthma. The three-dimensional structure at 2.2 A resolution of the active-site Cys25--&gt;Ser mutant presented here in an unliganded state provides further insight useful for the design of selective enzyme inhibitors.


==Overview==
Structure of a Cys25--&gt;Ser mutant of human cathepsin S.,Turkenburg JP, Lamers MB, Brzozowski AM, Wright LM, Hubbard RE, Sturt SL, Williams DH Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):451-5. Epub 2002, Feb 21. PMID:11856830<ref>PMID:11856830</ref>
Cathepsin S (EC 3.4.22.27), a cysteine proteinase of the papain superfamily, plays a critical role in the generation of a major histocompatibility complex (MHC) class II restricted T-cell response by antigen-presenting cells. Therefore, selective inhibition of this enzyme may be useful in modulating class II restricted T-cell responses in immune-related disorders such as rheumatoid arthritis, multiple sclerosis and extrinsic asthma. The three-dimensional structure at 2.2 A resolution of the active-site Cys25--&gt;Ser mutant presented here in an unliganded state provides further insight useful for the design of selective enzyme inhibitors.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1GLO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLO OCA].
</div>
<div class="pdbe-citations 1glo" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure of a Cys25--&gt;Ser mutant of human cathepsin S., Turkenburg JP, Lamers MB, Brzozowski AM, Wright LM, Hubbard RE, Sturt SL, Williams DH, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):451-5. Epub 2002, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11856830 11856830]
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
[[Category: Cathepsin S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brzozowski, A M.]]
[[Category: Brzozowski AM]]
[[Category: Hubbard, R E.]]
[[Category: Hubbard RE]]
[[Category: Lamers, M B.A C.]]
[[Category: Lamers MBAC]]
[[Category: Sturt, S L.]]
[[Category: Sturt SL]]
[[Category: Turkenburg, J P.]]
[[Category: Turkenburg JP]]
[[Category: Williams, D H.]]
[[Category: Williams DH]]
[[Category: Wright, L M.]]
[[Category: Wright LM]]
[[Category: Cathepsin s]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Proteinase]]
[[Category: Thiol protea]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:43:48 2008''

Latest revision as of 08:28, 6 November 2024

Crystal Structure of Cys25Ser mutant of human cathepsin S

1glo, resolution 2.20Å

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