1itp: Difference between revisions
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== | ==Solution Structure of POIA1== | ||
<StructureSection load='1itp' size='340' side='right'caption='[[1itp]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1itp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_ostreatus Pleurotus ostreatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ITP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ITP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1itp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1itp OCA], [https://pdbe.org/1itp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1itp RCSB], [https://www.ebi.ac.uk/pdbsum/1itp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1itp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PIA1_PLEOS PIA1_PLEOS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Solution structure of POIA1 (Pleurotus ostreatus proteinase A inhibitor 1), which functions as an intramolecular chaperone and as an inhibitor to subtilisin, was determined. By making use of the fact that POIA1 is the only structured protein that shows homology to the propeptide of subtilisin, which is unstructured by itself, foldability of this protein was elucidated. It became clear that the evolutionarily conserved residues play two important roles, one for the maintenance of its own structure, and the other for the interaction with subtilisin. Structural softness and mutational tolerance contained in the POIA1 structure makes it an ideal material for designing a foldable protein. | Solution structure of POIA1 (Pleurotus ostreatus proteinase A inhibitor 1), which functions as an intramolecular chaperone and as an inhibitor to subtilisin, was determined. By making use of the fact that POIA1 is the only structured protein that shows homology to the propeptide of subtilisin, which is unstructured by itself, foldability of this protein was elucidated. It became clear that the evolutionarily conserved residues play two important roles, one for the maintenance of its own structure, and the other for the interaction with subtilisin. Structural softness and mutational tolerance contained in the POIA1 structure makes it an ideal material for designing a foldable protein. | ||
Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperone.,Sasakawa H, Yoshinaga S, Kojima S, Tamura A J Mol Biol. 2002 Mar 15;317(1):159-67. PMID:11916386<ref>PMID:11916386</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1itp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pleurotus ostreatus]] | [[Category: Pleurotus ostreatus]] | ||
[[Category: Kojima S]] | |||
[[Category: Kojima | [[Category: Sasakawa H]] | ||
[[Category: Sasakawa | [[Category: Tamura A]] | ||
[[Category: Tamura | [[Category: Yoshinaga S]] | ||
[[Category: Yoshinaga | |||
Latest revision as of 18:42, 29 November 2023
Solution Structure of POIA1
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