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2ol2

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[[Image:2ol2.gif|left|200px]]
[[Image:2ol2.gif|left|200px]]
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{{Structure
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|PDB= 2ol2 |SIZE=350|CAPTION= <scene name='initialview01'>2ol2</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_2ol2", creates the "Structure Box" on the page.
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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])
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{{STRUCTURE_2ol2| PDB=2ol2 | SCENE= }}
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|RELATEDENTRY=[[2hi9|2HI9]], [[1lq8|1LQ8]]
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|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>
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'''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.]]
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[[Category: serpin]]
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[[Category: Serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:08:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:19 2008''
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Revision as of 08:08, 4 May 2008

Template:STRUCTURE 2ol2

High Resolution Structure of Native PCI in Space Group P21


Overview

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 Structure

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

Reference

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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