1ny2: Difference between revisions

Revision as of 21:49, 28 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:1ny2.png

Template:STRUCTURE 1ny2

Human alpha thrombin inhibited by RPPGF and hirugenHuman alpha thrombin inhibited by RPPGF and hirugen

Template:ABSTRACT PUBMED 12598231

About this StructureAbout this Structure

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

ReferenceReference

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 Mon Jul 28 21:49:24 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ny2.jpg|left|200px]]
+{{Seed}}
+[[Image:1ny2.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ny2|  PDB=1ny2  |  SCENE=  }}
-'''Human alpha thrombin inhibited by RPPGF and hirugen'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12598231}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12598231 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12598231}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Retro binding]]
 [[Category: Thrombosis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:07:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:49:24 2008''