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1tab

From Proteopedia

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[[Image:1tab.gif|left|200px]]<br /><applet load="1tab" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tab, resolution 2.3&Aring;" />
 
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'''STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN'''<br />
 
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==Overview==
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==STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN==
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The crystal structure of the complex formed by bovine trypsin and Bowman-Birk type protease inhibitor AB-I extracted from azuki beans (Vigna angularis) 'Takara' has been analyzed. The structure was solved by the application of the phase combination of single isomorphous phases and trypsin model phases, followed by phase improvement using the iterative Fourier technique. From the resulting electron density map, a three-dimensional atomic model of the trypsin binding domain of AB-I has been built. The peptide chain at the trypsin reactive site turns back sharply at Pro29 and forms a 9-residue ring (Cys24-Cys32). The 'front side' of this ring, consisting of the reactive site (Cys24-Met28), interacts with trypsin in a similar manner to other families of inhibitors and forms a stable complex, which seems to be maintained by the interactions with the 'back side' of this ring (Pro29-Cys34). The similar spatial arrangements of the 'back side' of this inhibitor and the 'secondary contact region' of the other inhibitors with respect to the reactive site suggest an important common role of these regions in exhibiting inhibitory activity.
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<StructureSection load='1tab' size='340' side='right'caption='[[1tab]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Vigna_angularis Vigna angularis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TAB 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=1tab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tab OCA], [https://pdbe.org/1tab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tab RCSB], [https://www.ebi.ac.uk/pdbsum/1tab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tab ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IBB1_PHAAN IBB1_PHAAN] Trypsin and chymotrypsin are inhibited simultaneously. There are two separate reactive sites for trypsin and chymotrypsin but they do not inhibit simultaneously.
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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/ta/1tab_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=1tab 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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1TAB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAB OCA].
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin., Tsunogae Y, Tanaka I, Yamane T, Kikkawa J, Ashida T, Ishikawa C, Watanabe K, Nakamura S, Takahashi K, J Biochem. 1986 Dec;100(6):1637-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3032921 3032921]
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[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Trypsin]]
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[[Category: Vigna angularis]]
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[[Category: Ashida, T.]]
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[[Category: Ashida T]]
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[[Category: Ishikawa, C.]]
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[[Category: Ishikawa C]]
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[[Category: Kikkawa, J I.]]
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[[Category: Kikkawa J-I]]
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[[Category: Nakamura, S.]]
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[[Category: Nakamura S]]
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[[Category: Takahashi, K.]]
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[[Category: Takahashi K]]
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[[Category: Tanaka, I.]]
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[[Category: Tanaka I]]
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[[Category: Tsunogae, Y.]]
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[[Category: Tsunogae Y]]
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[[Category: Watanabe, K.]]
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[[Category: Watanabe K]]
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[[Category: Yamane, T.]]
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[[Category: Yamane T]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:36 2008''
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Current revision

STRUCTURE OF THE TRYPSIN-BINDING DOMAIN OF BOWMAN-BIRK TYPE PROTEASE INHIBITOR AND ITS INTERACTION WITH TRYPSIN

PDB ID 1tab

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