2iln: Difference between revisions

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<StructureSection load='2iln' size='340' side='right'caption='[[2iln]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2iln' size='340' side='right'caption='[[2iln]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2iln]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin] and [https://en.wikipedia.org/wiki/Medsc Medsc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ILN FirstGlance]. <br>
<table><tr><td colspan='2'>[[2iln]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Medicago_scutellata Medicago scutellata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ILN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ILN FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mvz|1mvz]]</div></td></tr>
</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&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></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=2iln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iln OCA], [https://pdbe.org/2iln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iln RCSB], [https://www.ebi.ac.uk/pdbsum/2iln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iln ProSAT]</span></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=2iln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iln OCA], [https://pdbe.org/2iln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iln RCSB], [https://www.ebi.ac.uk/pdbsum/2iln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iln ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IBB_MEDSC IBB_MEDSC]] Inhibits trypsin but not chymotrypsin. Inhibits the trypsin-like proteinase activity present in larvae of the crop pests Adoxophyes orana, Hyphantria cunea, Lobesia botrana and Ostrinia nubilalis.<ref>PMID:9014368</ref> 
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/2iln_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/2iln_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 2iln" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2iln" style="background-color:#fffaf0;"></div>
==See Also==
*[[Trypsin 3D structures|Trypsin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bovin]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Medsc]]
[[Category: Trypsin]]
[[Category: Capaldi, S]]
[[Category: Carrizo, M E]]
[[Category: Faggion, B]]
[[Category: Monaco, H L]]
[[Category: Perduca, M]]
[[Category: Ragona, L]]
[[Category: Tava, A]]
[[Category: Bowman-birk inhibitor]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Medicago scutellata]]
[[Category: Medicago scutellata]]
[[Category: Protease inhibitor]]
[[Category: Capaldi S]]
[[Category: Carrizo ME]]
[[Category: Faggion B]]
[[Category: Monaco HL]]
[[Category: Perduca M]]
[[Category: Ragona L]]
[[Category: Tava A]]

Latest revision as of 04:04, 21 November 2024

Crystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsinCrystal structure of the Bowman-Birk inhibitor from snail medic seeds in complex with bovine trypsin

Structural highlights

2iln is a 3 chain structure with sequence from Bos taurus and Medicago scutellata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRY1_BOVIN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of the ternary complex of the anticarcinogenic Bowman-Birk protease inhibitor purified from snail medic (Medicago scutellata) seeds (MSTI) and two molecules of bovine trypsin has been solved by X-ray diffraction analysis of single crystals to a resolution of 2.0 A. This is the highest resolution model of a ternary complex of this type currently available. The two binding loops of the MSTI differ in only one amino acid and have in both cases an arginine in position P1. The distances between the residues of the inhibitor at the binding interface and the trypsin side chains that recognize them are almost identical in the two sites. When compared to the NMR model of the uncomplexed MSTI, the inhibitor in the functional assembly with trypsin shows the largest differences in the two P2' residues. Compared with the similar ternary complex of the soybean trypsin inhibitor, this model shows very small differences in the polypeptide chain of the trypsin binding sites and its largest difference in the area between Asp 26 and His 32 of the MSTI which in the soybean inhibitor has an extra Leu inserted in position 29.

Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin.,Capaldi S, Perduca M, Faggion B, Carrizo ME, Tava A, Ragona L, Monaco HL J Struct Biol. 2007 Apr;158(1):71-9. Epub 2006 Oct 26. PMID:17142058[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Capaldi S, Perduca M, Faggion B, Carrizo ME, Tava A, Ragona L, Monaco HL. Crystal structure of the anticarcinogenic Bowman-Birk inhibitor from snail medic (Medicago scutellata) seeds complexed with bovine trypsin. J Struct Biol. 2007 Apr;158(1):71-9. Epub 2006 Oct 26. PMID:17142058 doi:10.1016/j.jsb.2006.10.017

2iln, resolution 2.00Å

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OCA