2ol2: Difference between revisions

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[[Image:2ol2.gif|left|200px]]
[[Image:2ol2.gif|left|200px]]


{{Structure
<!--
|PDB= 2ol2 |SIZE=350|CAPTION= <scene name='initialview01'>2ol2</scene>, resolution 2.00&Aring;
The line below this paragraph, containing "STRUCTURE_2ol2", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|GENE= SERPINA5, PCI, PLANH3, PROCI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_2ol2|  PDB=2ol2 |  SCENE= }}  
|RELATEDENTRY=[[2hi9|2HI9]], [[1lq8|1LQ8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ol2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ol2 OCA], [http://www.ebi.ac.uk/pdbsum/2ol2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ol2 RCSB]</span>
}}


'''High Resolution Structure of Native PCI in Space Group P21'''
'''High Resolution Structure of Native PCI in Space Group P21'''
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[[Category: Huntington, J A.]]
[[Category: Huntington, J A.]]
[[Category: Li, W.]]
[[Category: Li, W.]]
[[Category: serpin]]
[[Category: Serpin]]
 
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Revision as of 11:08, 4 May 2008

File:2ol2.gif

Template:STRUCTURE 2ol2

High Resolution Structure of Native PCI in Space Group P21


OverviewOverview

Protein C inhibitor (PCI) is a multifunctional serpin with wide ranging protease inhibitory functions, unique cofactor binding activities, and potential non-inhibitory functions akin to the hormone-transporting serpins. To gain insight into the molecular mechanisms utilized by PCI we developed a robust expression system in Escherichia coli and solved the crystal structure of PCI in its native state. The five monomers obtained from our two crystal forms provide an NMR-like ensemble revealing regions of inherent flexibility. The reactive center loop (RCL) of PCI is long and highly flexible with no evidence of hinge region incorporation into beta-sheet A, as seen for other heparin-binding serpins. We adapted an extrinsic fluorescence method for determining dissociation constants for heparin and find that the N-terminal tail of PCI and residues adjacent to helix H are not involved in heparin binding. The minimal heparin length capable of tight binding to PCI was determined to be chains of eight monosaccharide units. A large hydrophobic pocket occupied by hydrophobic crystal contacts was found in an analogous position to the hormone-binding site in thyroxine-binding globulin. In conclusion, the data presented here provide important insights into the mechanisms by which PCI exercises its multiple inhibitory and non-inhibitory functions.

About this StructureAbout this Structure

2OL2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of native protein C inhibitor provides insight into its multiple functions., Li W, Adams TE, Kjellberg M, Stenflo J, Huntington JA, J Biol Chem. 2007 May 4;282(18):13759-68. Epub 2007 Mar 2. PMID:17337440 Page seeded by OCA on Sun May 4 11:08:15 2008

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