1itp
From Proteopedia
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| - | [[Image:1itp.jpg|left|200px]] | + | [[Image:1itp.jpg|left|200px]] |
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| - | '''Solution Structure of POIA1''' | + | {{Structure |
| + | |PDB= 1itp |SIZE=350|CAPTION= <scene name='initialview01'>1itp</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution Structure of POIA1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ITP is a [ | + | 1ITP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pleurotus_ostreatus Pleurotus ostreatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ITP OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11916386 11916386] |
[[Category: Pleurotus ostreatus]] | [[Category: Pleurotus ostreatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: propeptide]] | [[Category: propeptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:54:48 2008'' |
Revision as of 09:54, 20 March 2008
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Solution Structure of POIA1
Overview
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.
About this Structure
1ITP is a Single protein structure of sequence from Pleurotus ostreatus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:54:48 2008
