1zjk: Difference between revisions

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[[Image:1zjk.gif|left|200px]]
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[[Image:1zjk.png|left|200px]]


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{{STRUCTURE_1zjk|  PDB=1zjk  |  SCENE=  }}  
{{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===




==Overview==
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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.
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==Disease==
==Disease==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16040602 16040602]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16040602 16040602]
The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions., Harmat V, Gal P, Kardos J, Szilagyi K, Ambrus G, Vegh B, Naray-Szabo G, Zavodszky P, J Mol Biol. 2004 Oct 1;342(5):1533-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15364579 15364579]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Modular protein]]
[[Category: Modular protein]]
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Revision as of 13:20, 27 July 2008

File:1zjk.png

Template:STRUCTURE 1zjk

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

Template:ABSTRACT PUBMED 16040602

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

The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions., Harmat V, Gal P, Kardos J, Szilagyi K, Ambrus G, Vegh B, Naray-Szabo G, Zavodszky P, J Mol Biol. 2004 Oct 1;342(5):1533-46. PMID:15364579

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