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2pmw
From Proteopedia
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|PDB= 2pmw |SIZE=350|CAPTION= <scene name='initialview01'>2pmw</scene>, resolution 2.3Å | |PDB= 2pmw |SIZE=350|CAPTION= <scene name='initialview01'>2pmw</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PCSK9, NARC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PCSK9, NARC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pmw OCA], [http://www.ebi.ac.uk/pdbsum/2pmw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pmw RCSB]</span> | ||
}} | }} | ||
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[[Category: Thibault, S T.]] | [[Category: Thibault, S T.]] | ||
[[Category: Walker, N P.C.]] | [[Category: Walker, N P.C.]] | ||
| - | [[Category: SO4]] | ||
[[Category: propeptide]] | [[Category: propeptide]] | ||
[[Category: protease]] | [[Category: protease]] | ||
[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:38:08 2008'' |
Revision as of 01:38, 31 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PCSK9, NARC1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 04:38:08 2008
