1ny2

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[[Image:1ny2.jpg|left|200px]]
[[Image:1ny2.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1ny2 |SIZE=350|CAPTION= <scene name='initialview01'>1ny2</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1ny2", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=TYS:SULFONATED+TYROSINE'>TYS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ny2| PDB=1ny2 | SCENE= }}
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|RELATEDENTRY=[[1hdt|1HDT]], [[7kme|7KME]], [[8kme|8KME]], [[1tmu|1TMU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ny2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ny2 OCA], [http://www.ebi.ac.uk/pdbsum/1ny2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ny2 RCSB]</span>
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}}
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'''Human alpha thrombin inhibited by RPPGF and hirugen'''
'''Human alpha thrombin inhibited by RPPGF and hirugen'''
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[[Category: Tulinsky, A.]]
[[Category: Tulinsky, A.]]
[[Category: Warnock, M.]]
[[Category: Warnock, M.]]
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[[Category: retro binding]]
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[[Category: Retro binding]]
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[[Category: thrombosis]]
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[[Category: Thrombosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:07:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:37:06 2008''
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Revision as of 00:07, 3 May 2008

Image:1ny2.jpg

Template:STRUCTURE 1ny2

Human alpha thrombin inhibited by RPPGF and hirugen


Overview

Investigations determined the mechanism(s) by which Arg-Pro-Pro-Gly-Phe (RPPGF) inhibits thrombin-induced platelet activation. High concentrations of RPPGF inhibit thrombin-induced coagulant activity. RPPGF binds to the active site of thrombin by forming a parallel beta-strand with Ser214-Gly216 and interacts with His57, Asp189, and Ser195 of the catalytic triad. RPPGF competitively inhibits alpha-thrombin from hydrolyzing Sar-Pro-Arg-paranitroanilide with a Ki = 1.75 +/- 0.03 mM. Other mechanisms were sought to explain why RPPGF inhibits thrombin activation of platelets at concentrations below that which inhibits its active site. Soluble RPPGF blocks biotinylated NATLDPRSFLLR of the thrombin cleavage site on protease-activated receptor (PAR)1 from binding to the peptide RPPGC (IC50 = 20 microM). The soluble recombinant extracellular domain of PAR1 (rPAR1EC) blocks biotinylated RPPGF binding to rPAR1EC (IC50 = 50 microM) bound to microtiter plates, but rPAR1EC deletion mutants missing the sequence LDPR or PRSF do not. RPPGF and related forms prevent the thrombin-like enzyme thrombocytin from proteolyzing rPAR1EC at concentrations that do not block thrombocytin's active site. These studies indicate that RPPGF is a bifunctional inhibitor of thrombin: it binds to PAR1 to prevent thrombin cleavage at Arg41 and interacts with the active site of alpha-thrombin.

About this Structure

1NY2 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanisms of Arg-Pro-Pro-Gly-Phe inhibition of thrombin., Hasan AA, Warnock M, Nieman M, Srikanth S, Mahdi F, Krishnan R, Tulinsky A, Schmaier AH, Am J Physiol Heart Circ Physiol. 2003 Jul;285(1):H183-93. Epub 2003 Feb, 21. PMID:12598231 Page seeded by OCA on Sat May 3 03:07:07 2008

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