1zjk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1zjk.gif|left|200px]] | [[Image:1zjk.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1zjk", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1zjk| PDB=1zjk | SCENE= }} | |||
| | |||
}} | |||
'''Crystal structure of the zymogen catalytic region of human MASP-2''' | '''Crystal structure of the zymogen catalytic region of human MASP-2''' | ||
| Line 39: | Line 36: | ||
[[Category: Vegh, B.]] | [[Category: Vegh, B.]] | ||
[[Category: Zavodszky, P.]] | [[Category: Zavodszky, P.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[Category: | [[Category: Modular protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:42:21 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:42, 3 May 2008
Crystal structure of the zymogen catalytic region of human MASP-2
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: MASP2 deficiency OMIM:[605102]
About this StructureAbout this Structure
1ZJK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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