4b2a: Difference between revisions
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==Structure of the factor Xa-like trypsin variant triple-Ala (TGA) in complex with eglin C== | ==Structure of the factor Xa-like trypsin variant triple-Ala (TGA) in complex with eglin C== | ||
<StructureSection load='4b2a' size='340' side='right' caption='[[4b2a]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='4b2a' size='340' side='right'caption='[[4b2a]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b2a]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4b2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B2A FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</td></tr> | ||
<tr id=' | <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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4b2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2a OCA], [https://pdbe.org/4b2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b2a RCSB], [https://www.ebi.ac.uk/pdbsum/4b2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b2a ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4b2a" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Eglin|Eglin]] | *[[Eglin|Eglin]] | ||
*[[Trypsin|Trypsin]] | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Hirudo medicinalis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Menzel | [[Category: Menzel A]] | ||
[[Category: Neumann | [[Category: Neumann P]] | ||
[[Category: Stubbs | [[Category: Stubbs MT]] | ||
Latest revision as of 14:41, 20 December 2023
Structure of the factor Xa-like trypsin variant triple-Ala (TGA) in complex with eglin CStructure of the factor Xa-like trypsin variant triple-Ala (TGA) in complex with eglin C
Structural highlights
FunctionPublication Abstract from PubMedAbstract The energetics of macromolecular interactions are complex, particularly where protein flexibility is involved. Exploiting serendipitous differences in the plasticity of a series of closely related trypsin variants, we analyzed the enthalpic and entropic contributions accompanying interaction with L45K-eglin C. Binding of the four variants show significant differences in released heat, although the affinities vary little, in accordance with the principle of enthalpy-entropy compensation. Binding of the most disordered variant is almost entirely enthalpically driven, with practically no entropy change. As structures of the complexes reveal negligible differences in protein-inhibitor contacts, we conclude that solvent effects contribute significantly to binding affinities. Thermodynamic signatures in macromolecular interactions involving conformational flexibility.,Menzel A, Neumann P, Schwieger C, Stubbs MT Biol Chem. 2014 Jul 1;395(7-8):905-11. doi: 10.1515/hsz-2014-0177. PMID:25003391[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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