Mannan-binding lectin serine protease

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Revision as of 07:59, 20 December 2016

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Mannan-binding lectin serine protease (MASP) are proteases associated with mannan-binding lectin (MLB). The lectin pathway of complement is part of the innate immunity. The pathway activation occurs via recognition of pathogens by MBL followed by activation of MASP leading to activation of the complement system[1]. Disease Relevance Structural highlights

3D structures of mannan-binding lectin serine protease

Updated on 20-December-2016 {{#tree:id=OrganizedByTopic|openlevels=0|

• Mannan-building serine protease 1

• • 4aqb – hMASP-1 - human
    
  • 4igd – hMASP-1 catalytic domain (mutant)
    
  • 4djz – hMASP-1 chain A sushi domain, chain B catalytic domain + SGPI-2
    
  • 3gov – hMASP-1 chain A sushi domain, chain B catalytic domain
    
  • 3pob – rMASP-1 CUB2 domain + MBL collagen-like peptide - rat
    
  • 3poe, 3pof, 3pog, [[3pofi], 3poj – rMASP-1 CUB2 domain
    

• Mannan-building serine protease 2

• • 5jpm, 4fxg – hMASP-2 + complement C4-A
    
  • 3tvj – hMASP-2 chain A sushi 2 domain, chain B catalytic domain + SGPI-2
    
  • 1q3x – hMASP-2 catalytic domain
    
  • 1zjk – hMASP-2 catalytic domain (mutant)
    
  • 1nt0 – hMASP-1 CUB1-EGF-CUB2 domain
    

• Mannan-building serine protease 3

• • 4kkd – hMASP-3 (mutant)
    
  • 3dem – hMASP-3 CUB1-EGF-CUB2 domain
    
  • 4iw4 – MASP-3 catalytic domain + ecotin – Escherichia coli
    

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References

1. ↑ Thiel S, Jensen L, Degn SE, Nielsen HJ, Gal P, Dobo J, Jensenius JC. Mannan-binding lectin (MBL)-associated serine protease-1 (MASP-1), a serine protease associated with humoral pattern-recognition molecules: normal and acute-phase levels in serum and stoichiometry of lectin pathway components. Clin Exp Immunol. 2012 Jul;169(1):38-48. doi: 10.1111/j.1365-2249.2012.04584.x. PMID:22670777 doi:http://dx.doi.org/10.1111/j.1365-2249.2012.04584.x