5jb4: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==A simplified BPTI variant containing 21 alanines out 58 of residues== | |||
<StructureSection load='5jb4' size='340' side='right' caption='[[5jb4]], [[Resolution|resolution]] 1.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5jb4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JB4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JB4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jb5|5jb5]], [[5jb6|5jb6]], [[5jb7|5jb7]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jb4 OCA], [http://pdbe.org/5jb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jb4 RCSB], [http://www.ebi.ac.uk/pdbsum/5jb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jb4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report a thermodynamic and structural analysis of six extensively simplified bovine pancreatic trypsin inhibitor (BPTI) variants containing 19-24 alanines out of 58 residues. Differential scanning calorimetry indicated a two-state thermal unfolding, typical of a native protein with densely packed interior. Surprisingly, increasing the number of alanines induced enthalpy stabilization, which was however over-compensated by entropy destabilization. X-ray crystallography indicated that the alanine substitutions caused the recruitment of novel water molecules facilitating the formation of protein-water hydrogen bonds and improving the hydration shells around the alanine's methyl groups, both of which presumably contributed to enthalpy stabilization. There was a strong correlation between the number of water molecules and the thermodynamic parameters. Overall, our results demonstrate that, in contrast to our initial expectation, a protein sequence in which over 40% of the residues are alanines can retain a densely packed structure and undergo thermal denaturation with a large enthalpy change, mainly contributed by hydration. | |||
Crystal structures of highly simplified BPTIs provide insights into hydration-driven increase of unfolding enthalpy.,Islam MM, Yohda M, Kidokoro SI, Kuroda Y Sci Rep. 2017 Mar 7;7:41205. doi: 10.1038/srep41205. PMID:28266637<ref>PMID:28266637</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5jb4" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Islam, M M]] | |||
[[Category: 21 alanine]] | |||
[[Category: Bovine pancreatic trypsin inhibitor variant]] | |||
[[Category: Hydrolase inhibitor]] | |||
[[Category: Protein design]] | |||
[[Category: Sequence simplification]] | |||
