2PMW

The Crystal Structure of Proprotein convertase subtilisin kexin type 9 (PCSK9)

Summary for 2PMW

• Entry DOI: 10.2210/pdb2pmw/pdb
• Descriptor: Proprotein convertase subtilisin/kexin type 9, SULFATE ION, ... (4 entities in total)
• Functional Keywords: propeptide, subtilisin, protease, hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 71657.61

Authors

Piper, D.E.,Romanow, W.G.,Thibault, S.T.,Walker, N.P.C. (deposition date: 2007-04-23, release date: 2007-05-08, Last modification date: 2024-10-30)

Primary citation

Piper, D.E.,Jackson, S.,Liu, Q.,Romanow, W.G.,Shetterly, S.,Thibault, S.T.,Shan, B.,Walker, N.P.
The Crystal Structure of PCSK9: A Regulator of Plasma LDL-Cholesterol.
Structure, 15:545-552, 2007

PubMed Abstract: Proprotein convertase subtilisin kexin type 9 (PCSK9) has been shown to be involved in the regulation of extracellular levels of the low-density lipoprotien receptor (LDLR). Although PCSK9 is a subtilase, it has not been shown to degrade the LDLR, and its LDLR-lowering mechanism remains uncertain. Here we report the crystal structure of human PCSK9 at 2.3 A resolution. PCSK9 has subtilisin-like pro- and catalytic domains, and the stable interaction between these domains prevents access to PCSK9's catalytic site. The C-terminal domain of PCSK9 has a novel protein fold and may mediate protein-protein interactions. The structure of PCSK9 provides insight into its biochemical characteristics and biological function.

PubMed: 17502100
DOI: 10.1016/j.str.2007.04.004

Experimental method

X-RAY DIFFRACTION (2.3 Å)