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[[Image:1tnl.gif|left|200px]]
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{{STRUCTURE_1tnl|  PDB=1tnl  |  SCENE=  }}
'''PREDICTION OF NOVEL SERINE PROTEASE INHIBITORS'''


==PREDICTION OF NOVEL SERINE PROTEASE INHIBITORS==
<StructureSection load='1tnl' size='340' side='right'caption='[[1tnl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tnl]] 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=1TNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TNL 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TPA:TRANS-2-PHENYLCYCLOPROPYLAMINE'>TPA</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=1tnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tnl OCA], [https://pdbe.org/1tnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tnl RCSB], [https://www.ebi.ac.uk/pdbsum/1tnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tnl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
== 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/tn/1tnl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1tnl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We describe here the use of a rapid computational method to predict the relative binding strengths of a series of small-molecule ligands for the serine proteinase trypsin. Flexible molecular models of the ligands were docked to the proteinase using an all-atom potential set, without cutoff limits for the non-bonded and electrostatic energies. The binding-strength calculation is done directly in terms of a molecular mechanics potential. The binding of eighteen different compounds, including non-binding controls, has been successfully predicted. The measured Ki is correlated with the predicted energy. The correctness of the theoretical calculations is demonstrated with both kinetics measurements and X-ray structure determination of six enzyme-inhibitor complexes.


==Overview==
Prediction of new serine proteinase inhibitors.,Kurinov IV, Harrison RW Nat Struct Biol. 1994 Oct;1(10):735-43. PMID:7634078<ref>PMID:7634078</ref>
We describe here the use of a rapid computational method to predict the relative binding strengths of a series of small-molecule ligands for the serine proteinase trypsin. Flexible molecular models of the ligands were docked to the proteinase using an all-atom potential set, without cutoff limits for the non-bonded and electrostatic energies. The binding-strength calculation is done directly in terms of a molecular mechanics potential. The binding of eighteen different compounds, including non-binding controls, has been successfully predicted. The measured Ki is correlated with the predicted energy. The correctness of the theoretical calculations is demonstrated with both kinetics measurements and X-ray structure determination of six enzyme-inhibitor complexes.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1TNL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNL OCA].
</div>
<div class="pdbe-citations 1tnl" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Prediction of new serine proteinase inhibitors., Kurinov IV, Harrison RW, Nat Struct Biol. 1994 Oct;1(10):735-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7634078 7634078]
*[[Trypsin 3D structures|Trypsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Trypsin]]
[[Category: Harrison RW]]
[[Category: Harrison, R W.]]
[[Category: Kurinov I]]
[[Category: Kurinov, I.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:09:43 2008''
Retrieved from "https://proteopedia.org/1tnl"