2hi9
From Proteopedia
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'''Crystal Structure of human native protein C inhibitor''' | '''Crystal Structure of human native protein C inhibitor''' | ||
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[[Category: Huntington, J A.]] | [[Category: Huntington, J A.]] | ||
[[Category: Li, W.]] | [[Category: Li, W.]] | ||
| - | [[Category: | + | [[Category: Acrosin inhibitor]] |
| - | [[Category: | + | [[Category: Activated protein c inhibitor]] |
| - | [[Category: | + | [[Category: Coagulation]] |
| - | [[Category: | + | [[Category: Haemostasis]] |
| - | [[Category: | + | [[Category: Serine protease inhibitor]] |
| - | [[Category: | + | [[Category: Serpin]] |
| - | [[Category: | + | [[Category: Thrombin inhibitor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:19:44 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:19, 4 May 2008
Crystal Structure of human native protein C inhibitor
Contents |
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.
Disease
Known disease associated with this structure: Protein C inhibitor deficiency OMIM:[601841]
About this Structure
2HI9 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 06:19:44 2008
