4b1t: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4b1t' size='340' side='right'caption='[[4b1t]], [[Resolution|resolution]] 1.78Å' scene=''> | <StructureSection load='4b1t' size='340' side='right'caption='[[4b1t]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b1t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4b1t]] 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=4B1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B1T 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]] 1.78Å</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=4b1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1t OCA], [https://pdbe.org/4b1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b1t RCSB], [https://www.ebi.ac.uk/pdbsum/4b1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b1t 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=4b1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1t OCA], [https://pdbe.org/4b1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b1t RCSB], [https://www.ebi.ac.uk/pdbsum/4b1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b1t ProSAT]</span></td></tr> | ||
</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 28: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Hirudo medicinalis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Menzel A]] | |||
[[Category: Menzel | [[Category: Neumann P]] | ||
[[Category: Neumann | [[Category: Stubbs MT]] | ||
[[Category: Stubbs | |||
Latest revision as of 14:41, 20 December 2023
Structure of the factor Xa-like trypsin variant triple-Ala (TA) in complex with eglin CStructure of the factor Xa-like trypsin variant triple-Ala (TA) 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
|
| ||||||||||||||||||