1hym: Difference between revisions
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New page: left|200px<br /><applet load="1hym" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hym" /> '''HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMI... |
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== | ==HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)== | ||
Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima | <StructureSection load='1hym' size='340' side='right'caption='[[1hym]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1hym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=1hym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hym OCA], [https://pdbe.org/1hym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hym RCSB], [https://www.ebi.ac.uk/pdbsum/1hym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hym ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ITH5_CUCMA ITH5_CUCMA] Specifically inhibits both trypsin and activated Hageman factor. | |||
== 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/hy/1hym_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=1hym ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In comparison to the intact form, CMTI-V* exhibited markedly reduced inhibitory properties and binding affinities toward trypsin and human blood coagulation factor XIIa. The equilibrium constant of trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3 kcal.mol-1). From the temperature dependence of delta G degrees, the following thermodynamic parameters were estimated: delta H degrees = 1.6 kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the functional and thermodynamic differences between the two forms, the three-dimensional solution structure of CMTI-V* was determined by a combined approach of NMR, distance geometry, and simulated annealing methods. Thus, following sequence-specific and stereospecific resonance assignments, including those of beta-, gamma-, delta-, and epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances and 123 dihedral angle constraints were determined, resulting in the computation and energy-minimization of 20 structures for CMTI-V*. The average root mean squared deviation in position for equivalent atoms between the 20 individual structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS) | |||
Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure.,Cai M, Gong Y, Prakash O, Krishnamoorthi R Biochemistry. 1995 Sep 26;34(38):12087-94. PMID:7547948<ref>PMID:7547948</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1hym" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cucurbita maxima]] | [[Category: Cucurbita maxima]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cai | [[Category: Cai M]] | ||
[[Category: Gong | [[Category: Gong Y]] | ||
[[Category: Krishnamoorthi | [[Category: Krishnamoorthi R]] | ||
[[Category: Prakash | [[Category: Prakash O]] | ||
