1itp: Difference between revisions

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[[Image:1itp.jpg|left|200px]]<br /><applet load="1itp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1itp.jpg|left|200px]]<br /><applet load="1itp" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1itp" />

'''Solution Structure of POIA1'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pleurotus_ostreatus Pleurotus ostreatus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ITP OCA].

1ITP is a [http://en.wikipedia.org/wiki/Single_protein 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==

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[[Category: propeptide]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:39:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:31 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1itp.jpg|left|200px]]<br /><applet load="1itp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1itp.jpg|left|200px]]<br /><applet load="1itp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1itp" />
 '''Solution Structure of POIA1'''<br />
 ==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.
+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==
-ITP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pleurotus_ostreatus Pleurotus ostreatus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ITP OCA].
+ITP is a [http://en.wikipedia.org/wiki/Single_protein 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==
@@ Line 21: / Line 21: @@
 [[Category: propeptide]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:39:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:31 2008''