2pmw

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17502100 17502100]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17502100 17502100]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Piper, D.E.]]
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[[Category: Piper, D E.]]
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[[Category: Romanow, W.G.]]
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[[Category: Romanow, W G.]]
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[[Category: Thibault, S.T.]]
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[[Category: Thibault, S T.]]
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[[Category: Walker, N.P.C.]]
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[[Category: Walker, N P.C.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: propeptide]]
[[Category: propeptide]]
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[[Category: subtilisin]]
[[Category: subtilisin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:09 2008''

Revision as of 16:31, 21 February 2008


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 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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