This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1zjk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zjk.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zjk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{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==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16040602}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16040602 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16040602}}
==Disease==
==Disease==
Line 23: Line 27:
==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]]
Line 38: Line 44:
[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Modular protein]]
[[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 Sun Jul 27 13:20:26 2008''

Revision as of 10:20, 27 July 2008

Image:1zjk.png

Template:STRUCTURE 1zjk

Contents

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

Template:ABSTRACT PUBMED 16040602

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

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

Page seeded by OCA on Sun Jul 27 13:20:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zjk"
Personal tools