2pai
From Proteopedia
(Difference between revisions)
(8 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
{{Theoretical_model}} | {{Theoretical_model}} | ||
- | {{Seed}} | ||
- | [[Image:2pai.png|left|200px]] | ||
- | < | + | ==ELUCIDATING THE STRUCTURAL CHEMISTRY OF GLYCOSAMINOGLYCAN RECOGNITION BY PROTEIN C INHIBITOR== |
- | + | <StructureSection load='2pai' size='340' side='right'caption='[[2pai]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PAI FirstGlance]. <br> | |
- | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pai FirstGlance], [https://www.ebi.ac.uk/pdbsum/2pai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pai ProSAT]</span></td></tr> | |
- | -- | + | </table> |
- | + | <div style="background-color:#fffaf0;"> | |
+ | == Publication Abstract from PubMed == | ||
+ | Glycosaminoglycans (GAGs) including heparin accelerate the inhibition of serine proteases by serine protease inhibitors (serpins), an essential process in regulating blood coagulation. to analyze the molecular basis for GAG recognition by the plasma serpin protein C inhibitor (PCI; also known as plasminogen activator inhibitor 3), we have constructed a complete, energy-minimized, three-dimensional model of PCI by using the structure of homologous alpha 1-antitrypsin as a template. Sequence analysis, hydrogen-bonding environment, and shape complementarity suggested that the N-terminal residues of PCI, which are not homologous to those of alpha 1-antitrypsin, form an amphipathic alpha-helix, here designated A+ since it precedes the alpha 1-antitrypsin A helix. Electrostatic calculations revealed a single, highly positive surface region arising from both the A+ and H helices, suggesting that this two-helix motif is required for GAG binding by PCI. The dominant role of electrostatic interactions in PCI-heparin binding was confirmed by the strong ionic strength dependence of heparin stimulation. The involvement of the A+ helix in heparin binding was verified by demonstrating that an anti-PCI antibody that specifically binds the A+ peptide blocks heparin binding. | ||
- | + | Elucidating the structural chemistry of glycosaminoglycan recognition by protein C inhibitor.,Kuhn LA, Griffin JH, Fisher CL, Greengard JS, Bouma BN, Espana F, Tainer JA Proc Natl Acad Sci U S A. 1990 Nov;87(21):8506-10. PMID:2172989<ref>PMID:2172989</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2pai" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Theoretical Model]] |
- | + | [[Category: Large Structures]] | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Fisher, C L]] | [[Category: Fisher, C L]] | ||
[[Category: Greengard, J S]] | [[Category: Greengard, J S]] | ||
Line 30: | Line 27: | ||
[[Category: Kuhn, L A]] | [[Category: Kuhn, L A]] | ||
[[Category: Tainer, J A]] | [[Category: Tainer, J A]] | ||
- | |||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:15:48 2010'' |
Current revision
Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution. |
ELUCIDATING THE STRUCTURAL CHEMISTRY OF GLYCOSAMINOGLYCAN RECOGNITION BY PROTEIN C INHIBITOR
|