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1qdq

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X-RAY CRYSTAL STRUCTURE OF BOVINE CATHEPSIN B-CA074 COMPLEX

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Retrieved from "http://52.214.119.220/wiki/index.php/1qdq"

Categories: Bos taurus | Large Structures | Yamamoto A

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-[[Image:1qdq.jpg|left|200px]]<br /><applet load="1qdq" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qdq, resolution 2.18&Aring;" />
-'''X-RAY CRYSTAL STRUCTURE OF BOVINE CATHEPSIN B-CA074 COMPLEX'''<br />
-==Overview==
+==X-RAY CRYSTAL STRUCTURE OF BOVINE CATHEPSIN B-CA074 COMPLEX==
-The crystal structure of the bovine spleen cathepsin B (BSCB)-CA074, complex was refined to R = 0.152 using X-ray diffraction data up to 2.18 A, resolution. BSCB is characterized by an extra Cys148-Cys252 disulfide, bridge, as compared with rat and human CBs. Although the crystal, structures of these enzymes showed similar overall folding, a difference, was observed in the occluding loop, a structural element specific only to, CB. Comparison of the torsion angles indicated the different flexibilities, of their loop structures. The oxirane C6 atom of CA074 was covalently, bonded to the Cys29 S(gamma) atom (C3-S(gamma)=1.81 A), where the, S-configuration was transformed to the R-form. Concerning the oxirane, carbon atom that participates in the covalent bonding with the Cys, residue, an acceptable rule has been proposed. The substrate specificities, at the Sn (n = 1-3) and Sn' (n=1 and 2) subsites of CB, together with the, interaction features as to CA074, have been discussed in comparison with, the crystal structure of the papain-CA028 (a CA074-related inhibitor), complex.
+<StructureSection load='1qdq' size='340' side='right'caption='[[1qdq]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qdq]] is a 1 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=1QDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QDQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=074:[PROPYLAMINO-3-HYDROXY-BUTAN-1,4-DIONYL]-ISOLEUCYL-PROLINE'>074</scene></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=1qdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdq OCA], [https://pdbe.org/1qdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qdq RCSB], [https://www.ebi.ac.uk/pdbsum/1qdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qdq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CATB_BOVIN CATB_BOVIN] Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qd/1qdq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1qdq ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-QDQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with 074 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cathepsin_B Cathepsin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.1 3.4.22.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QDQ OCA].
+*[[Cathepsin 3D structures|Cathepsin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex., Yamamoto A, Tomoo K, Hara T, Murata M, Kitamura K, Ishida T, J Biochem (Tokyo). 2000 Apr;127(4):635-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10739956 10739956]
 [[Category: Bos taurus]]
-[[Category: Cathepsin B]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Yamamoto A]]
-[[Category: Yamamoto, A.]]
-[[Category: 074]]
-[[Category: cathepsin b]]
-[[Category: cathepsin b-specific inhibitor complex]]
-[[Category: papain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:36:22 2007''

1qdq

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X-RAY CRYSTAL STRUCTURE OF BOVINE CATHEPSIN B-CA074 COMPLEX

Structural highlights

Function

Evolutionary Conservation

See Also

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