6EUA

The fibrinogen-like domain of human Angptl3

Summary for 6EUA

• Entry DOI: 10.2210/pdb6eua/pdb
• Descriptor: Angiopoietin-related protein 3 (2 entities in total)
• Functional Keywords: lipid metabolism, plasma triglyceride, angiopoietin-like, coronary artery disease, signaling protein
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted : Q9Y5C1
• Total number of polymer chains: 3
• Total formula weight: 80120.24

Authors

Biterova, E.I.,Esmaeeli, M.E.,Alanen, H.I.,Saaranen, M.,Ruddock, L.W. (deposition date: 2017-10-30, release date: 2018-05-09, Last modification date: 2024-11-20)

Primary citation

Biterova, E.,Esmaeeli, M.,Alanen, H.I.,Saaranen, M.,Ruddock, L.W.
Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease.
Sci Rep, 8:6752-6752, 2018

PubMed Abstract: Coronary artery disease is the most common cause of death globally and is linked to a number of risk factors including serum low density lipoprotein, high density lipoprotein, triglycerides and lipoprotein(a). Recently two proteins, angiopoietin-like protein 3 and 4, have emerged from genetic studies as being factors that significantly modulate plasma triglyceride levels and coronary artery disease. The exact function and mechanism of action of both proteins remains to be elucidated, however, mutations in these proteins results in up to 34% reduction in coronary artery disease and inhibition of function results in reduced plasma triglyceride levels. Here we report the crystal structures of the fibrinogen-like domains of both proteins. These structures offer new insights into the reported loss of function mutations, the mechanisms of action of the proteins and open up the possibility for the rational design of low molecular weight inhibitors for intervention in coronary artery disease.

PubMed: 29713054
DOI: 10.1038/s41598-018-25237-7

Experimental method

X-RAY DIFFRACTION (2.095 Å)