4b2a: Difference between revisions

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-'''Unreleased structure'''
-The entry 4b2a is ON HOLD  until sometime in the future
+==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]] 1.89&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#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=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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Abstract 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.
-Authors: Menzel, A., Neumann, P., Stubbs, M.T.
+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<ref>PMID:25003391</ref>
-Description: Structure of the factor Xa-like trypsin variant triple-Ala (TGA) in complex with eglin C
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4b2a" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Eglin|Eglin]]
+*[[Trypsin 3D structures|Trypsin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bos taurus]]
+[[Category: Hirudo medicinalis]]
+[[Category: Large Structures]]
+[[Category: Menzel A]]
+[[Category: Neumann P]]
+[[Category: Stubbs MT]]