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2pmw
From Proteopedia
(New page: 200px<br /> <applet load="2pmw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pmw, resolution 2.3Å" /> '''The Crystal Structur...) |
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| - | [[Image:2pmw. | + | [[Image:2pmw.jpg|left|200px]]<br /><applet load="2pmw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2pmw" size=" | + | |
caption="2pmw, resolution 2.3Å" /> | caption="2pmw, resolution 2.3Å" /> | ||
'''The Crystal Structure of Proprotein convertase subtilisin kexin type 9 (PCSK9)'''<br /> | '''The Crystal Structure of Proprotein convertase subtilisin kexin type 9 (PCSK9)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PMW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2PMW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PMW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:50 2008'' |
Revision as of 13:09, 23 January 2008
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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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