1zjk
From Proteopedia
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- | [[Image:1zjk.png|left|200px]] | ||
- | < | + | ==Crystal structure of the zymogen catalytic region of human MASP-2== |
- | + | <StructureSection load='1zjk' size='340' side='right'caption='[[1zjk]], [[Resolution|resolution]] 2.18Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1zjk]] 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=1ZJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZJK 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]] 2.18Å</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=1zjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zjk OCA], [https://pdbe.org/1zjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zjk RCSB], [https://www.ebi.ac.uk/pdbsum/1zjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zjk ProSAT]</span></td></tr> |
- | + | </table> | |
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/MASP2_HUMAN MASP2_HUMAN] Defects in MASP2 are the cause of MASP2 deficiency (MASPD) [MIM:[https://omim.org/entry/613791 613791]. MASPD is a disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease.<ref>PMID:12904520</ref> <ref>PMID:17252003</ref> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/MASP2_HUMAN MASP2_HUMAN] Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.<ref>PMID:10946292</ref> | ||
+ | == 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/zj/1zjk_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=1zjk ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Few reports have described in detail a true autoactivation process, where no extrinsic cleavage factors are required to initiate the autoactivation of a zymogen. Herein, we provide structural and mechanistic insight into the autoactivation of a multidomain serine protease: mannose-binding lectin-associated serine protease-2 (MASP-2), the first enzymatic component in the lectin pathway of complement activation. We characterized the proenzyme form of a MASP-2 catalytic fragment encompassing its C-terminal three domains and solved its crystal structure at 2.4 A resolution. Surprisingly, zymogen MASP-2 is capable of cleaving its natural substrate C4, with an efficiency about 10% that of active MASP-2. Comparison of the zymogen and active structures of MASP-2 reveals that, in addition to the activation domain, other loops of the serine protease domain undergo significant conformational changes. This additional flexibility could play a key role in the transition of zymogen MASP-2 into a proteolytically active form. Based on the three-dimensional structures of proenzyme and active MASP-2 catalytic fragments, we present model for the active zymogen MASP-2 complex and propose a mechanism for the autoactivation process. | ||
- | + | A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations.,Gal P, Harmat V, Kocsis A, Bian T, Barna L, Ambrus G, Vegh B, Balczer J, Sim RB, Naray-Szabo G, Zavodszky P J Biol Chem. 2005 Sep 30;280(39):33435-44. Epub 2005 Jul 21. PMID:16040602<ref>PMID:16040602</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1zjk" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Mannan-binding lectin serine protease|Mannan-binding lectin serine protease]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
- | [[ | + | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Ambrus | + | [[Category: Large Structures]] |
- | [[Category: Balczer | + | [[Category: Ambrus G]] |
- | [[Category: Barna | + | [[Category: Balczer J]] |
- | [[Category: Bian | + | [[Category: Barna L]] |
- | [[Category: Gal | + | [[Category: Bian T]] |
- | [[Category: Harmat | + | [[Category: Gal P]] |
- | [[Category: Kocsis | + | [[Category: Harmat V]] |
- | [[Category: Naray-Szabo | + | [[Category: Kocsis A]] |
- | [[Category: Sim | + | [[Category: Naray-Szabo G]] |
- | [[Category: Vegh | + | [[Category: Sim RB]] |
- | [[Category: Zavodszky | + | [[Category: Vegh B]] |
- | + | [[Category: Zavodszky P]] | |
- | + | ||
- | + |
Current revision
Crystal structure of the zymogen catalytic region of human MASP-2
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Categories: Homo sapiens | Large Structures | Ambrus G | Balczer J | Barna L | Bian T | Gal P | Harmat V | Kocsis A | Naray-Szabo G | Sim RB | Vegh B | Zavodszky P