2ol2: Difference between revisions

Revision as of 21:08, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ol2.png

Template:STRUCTURE 2ol2

High Resolution Structure of Native PCI in Space Group P21High Resolution Structure of Native PCI in Space Group P21

Template:ABSTRACT PUBMED 17337440

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

Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation., Huntington JA, Kjellberg M, Stenflo J, Structure. 2003 Feb;11(2):205-15. PMID:12575940

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-'''High Resolution Structure of Native PCI in Space Group P21'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17337440}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17337440 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17337440}}
 ==About this Structure==
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 ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17337440 17337440]
+Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation., Huntington JA, Kjellberg M, Stenflo J, Structure. 2003 Feb;11(2):205-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12575940 12575940]
 [[Category: Homo sapiens]]
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 [[Category: Li, W.]]
 [[Category: Serpin]]
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