1zjk

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[[Image:1zjk.gif|left|200px]]
[[Image:1zjk.gif|left|200px]]
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{{Structure
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|PDB= 1zjk |SIZE=350|CAPTION= <scene name='initialview01'>1zjk</scene>, resolution 2.18&Aring;
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The line below this paragraph, containing "STRUCTURE_1zjk", creates the "Structure Box" on the page.
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|GENE= MASP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1zjk| PDB=1zjk | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zjk OCA], [http://www.ebi.ac.uk/pdbsum/1zjk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zjk RCSB]</span>
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'''Crystal structure of the zymogen catalytic region of human MASP-2'''
'''Crystal structure of the zymogen catalytic region of human MASP-2'''
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[[Category: Vegh, B.]]
[[Category: Vegh, B.]]
[[Category: Zavodszky, P.]]
[[Category: Zavodszky, P.]]
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[[Category: beta barrel]]
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[[Category: modular protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:42:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:37:34 2008''
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Revision as of 14:42, 3 May 2008

Image:1zjk.gif

Template:STRUCTURE 1zjk

Crystal structure of the zymogen catalytic region of human MASP-2


Contents

Overview

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.

Disease

Known disease associated with this structure: MASP2 deficiency OMIM:[605102]

About this Structure

1ZJK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 17:42:21 2008

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OCA

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