1itp

Solution Structure of POIA1

spinqualitylabelsall models 1itp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1itp is a 1 chain structure with sequence from Pleurotus ostreatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PIA1_PLEOS 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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