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1mkw

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(New page: 200px<br /><applet load="1mkw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mkw, resolution 2.3&Aring;" /> '''THE CO-CRYSTAL STRUCT...)
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[[Image:1mkw.jpg|left|200px]]<br /><applet load="1mkw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mkw, resolution 2.3&Aring;" />
 
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'''THE CO-CRYSTAL STRUCTURE OF UNLIGANDED BOVINE ALPHA-THROMBIN AND PRETHROMBIN-2: MOVEMENT OF THE YPPW SEGMENT AND ACTIVE SITE RESIDUES UPON LIGAND BINDING'''<br />
 
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==Overview==
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==THE CO-CRYSTAL STRUCTURE OF UNLIGANDED BOVINE ALPHA-THROMBIN AND PRETHROMBIN-2: MOVEMENT OF THE YPPW SEGMENT AND ACTIVE SITE RESIDUES UPON LIGAND BINDING==
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Unliganded bovine alpha-thrombin and prethrombin-2 have been, co-crystallized, in space group P21212, using either ammonium sulfate or, polyethylene glycol 2000 (PEG2K), and their structures determined at 2.2 A, and 2.3 A, respectively. Initial phases were determined by molecular, replacement and refined using XPLOR to final R factors of 0.187 (Rfree =, 0.255) and 0.190 (Rfree = 0.282) for the salt and PEG2K models, respectively. The apo-enzyme form of bovine alpha-thrombin shows dramatic, shifts in placement for the Tyr-Pro-Pro-Trp segment, for Glu-192, and for, the catalytic residues His-57 and Ser-195, when compared to 4 thrombin, complexes representing different states of catalysis, namely (1) the, Michaelis complex (residues 7-19 of fibrinogen A alpha with a, non-cleavable scissile bond), (2) enzyme-inhibitor complex (D-Phe-Pro-Arg, chloromethylketone), (3) enzyme product complex (residues 7-16 of, fibrinopeptide A), and (4) the exosite complex (residues 53-64 of, hirudin). The structures of bovine and human prethrombin-2 are generally, similar to one another (RMS deviation of 0.68 A) but differ significantly, in the Arg-15/Ile-16 cleavage region and in the three activation domains, which are disordered in bovine prethrombin-2, analogous to that seen for, trypsinogen.
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<StructureSection load='1mkw' size='340' side='right'caption='[[1mkw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mkw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkw OCA], [https://pdbe.org/1mkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mkw RCSB], [https://www.ebi.ac.uk/pdbsum/1mkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THRB_BOVIN THRB_BOVIN] Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mkw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mkw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MKW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MKW OCA].
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*[[Thrombin 3D Structures|Thrombin 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand binding., Malkowski MG, Martin PD, Guzik JC, Edwards BF, Protein Sci. 1997 Jul;6(7):1438-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9232645 9232645]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Thrombin]]
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[[Category: Edwards BFP]]
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[[Category: Edwards, B.F.P.]]
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[[Category: Malkowski MG]]
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[[Category: Malkowski, M.G.]]
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[[Category: complex (blood coagulation/proenzyme)]]
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[[Category: plasma]]
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[[Category: prethrombin-2]]
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[[Category: serine protease]]
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[[Category: thrombin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:29:15 2007''
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Current revision

THE CO-CRYSTAL STRUCTURE OF UNLIGANDED BOVINE ALPHA-THROMBIN AND PRETHROMBIN-2: MOVEMENT OF THE YPPW SEGMENT AND ACTIVE SITE RESIDUES UPON LIGAND BINDING

PDB ID 1mkw

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