2pmw

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(New page: 200px<br /> <applet load="2pmw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pmw, resolution 2.3&Aring;" /> '''The Crystal Structur...)
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Revision as of 21:18, 12 November 2007


2pmw, resolution 2.3Å

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

Overview

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.

About this Structure

2PMW is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

The Crystal Structure of PCSK9: A Regulator of Plasma LDL-Cholesterol., Piper DE, Jackson S, Liu Q, Romanow WG, Shetterly S, Thibault ST, Shan B, Walker NP, Structure. 2007 May;15(5):545-52. PMID:17502100

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