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1hrt

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(New page: 200px<br /><applet load="1hrt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrt, resolution 2.8&Aring;" /> '''THE STRUCTURE OF A CO...)
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[[Image:1hrt.gif|left|200px]]<br /><applet load="1hrt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hrt, resolution 2.8&Aring;" />
 
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'''THE STRUCTURE OF A COMPLEX OF BOVINE ALPHA-THROMBIN AND RECOMBINANT HIRUDIN AT 2.8 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==THE STRUCTURE OF A COMPLEX OF BOVINE ALPHA-THROMBIN AND RECOMBINANT HIRUDIN AT 2.8 ANGSTROMS RESOLUTION==
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Crystals of the complex of bovine alpha-thrombin with recombinant hirudin, variant 1 have space group C222(1) with cell constants a = 59.11, b =, 102.62, and c = 143.26 A. The orientation and position of the thrombin, component was determined by molecular replacement and the hirudin molecule, was fit in 2 magnitude of Fo - magnitude of Fc electron density maps. The, structure was refined by restrained least squares and simulated annealing, to R = 0.161 at 2.8-A resolution. The binding of hirudin to thrombin is, generally similar to that observed in the crystals of human, thrombin-hirudin. Several differences in the interactions of the, COOH-terminal polypeptide of hirudin, specifically of residues Asp-55h, Phe-56h, Glu-57h, and Glu-58h, and a few differences in the interactions, of the hirudin core, specifically of residues Asp-5h, Ser-19h, and, Asn-20h, with thrombin from human thrombin-hirudin suggest that there is, some flexibility in the binding of these 2 molecules. Most of the residues, in the 9 subsites that bind fibrinopeptide A7-16 to thrombin also interact, with the NH2-terminal domain of hirudin. The S1 subsite is a notable, exception in that only 1 of its 6 residues, namely Ser-214, interacts with, hirudin. The only difference between human and bovine thrombins that, appears to influence the binding of hirudin is the replacement of Lys-149E, by an acidic glutamate in the bovine enzyme.
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<StructureSection load='1hrt' size='340' side='right'caption='[[1hrt]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hrt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRT 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]] 2.8&#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=1hrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hrt OCA], [https://pdbe.org/1hrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hrt RCSB], [https://www.ebi.ac.uk/pdbsum/1hrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hrt 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/hr/1hrt_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=1hrt 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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1HRT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. 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=1HRT OCA].
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*[[Hirudin 3D structures|Hirudin 3D structures]]
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*[[Thrombin 3D Structures|Thrombin 3D Structures]]
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==Reference==
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__TOC__
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The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution., Vitali J, Martin PD, Malkowski MG, Robertson WD, Lazar JB, Winant RC, Johnson PH, Edwards BF, J Biol Chem. 1992 Sep 5;267(25):17670-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1517214 1517214]
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
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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: Vitali J]]
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[[Category: Vitali, J.]]
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[[Category: hydrolase(serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:47:28 2007''
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Current revision

THE STRUCTURE OF A COMPLEX OF BOVINE ALPHA-THROMBIN AND RECOMBINANT HIRUDIN AT 2.8 ANGSTROMS RESOLUTION

PDB ID 1hrt

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