1ag2: Difference between revisions

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[[Image:1ag2.gif|left|200px]]<br /><applet load="1ag2" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ag2.gif|left|200px]]<br /><applet load="1ag2" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ag2" />

'''PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE'''<br />

==Overview==

The 'protein only' hypothesis states that a modified form of normal prion, protein triggers infectious neurodegenerative diseases, such as bovine, spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in, humans. Prion proteins are thought to exist in two different, conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential, for understanding the transition to PrPsc. The nuclear magnetic resonance, (NMR) structure of the autonomously folding PrP domain comprising residues, 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three, alpha-helices. This domain contains most of the point-mutation sites that, have been linked, in human PrP, to the occurrence of familial prion, diseases. The NMR structure shows that these mutations occur within, or, directly adjacent to, regular secondary structures. The presence of a, beta-sheet in PrP(121-231) is in contrast with model predictions of an, all-helical structure of PrPc (ref. 8), and may be important for the, initiation of the transition from PrPc to PrPsc.

The 'protein only' hypothesis states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain comprising residues 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three alpha-helices. This domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases. The NMR structure shows that these mutations occur within, or directly adjacent to, regular secondary structures. The presence of a beta-sheet in PrP(121-231) is in contrast with model predictions of an all-helical structure of PrPc (ref. 8), and may be important for the initiation of the transition from PrPc to PrPsc.

==About this Structure==

1AG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1AG2 OCA].

1AG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AG2 OCA].

==Reference==

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[[Category: prion protein]]

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@@ Line 1: / Line 1: @@
-[[Image:1ag2.gif|left|200px]]<br /><applet load="1ag2" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ag2.gif|left|200px]]<br /><applet load="1ag2" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ag2" />
 '''PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, 2 MINIMIZED AVERAGE STRUCTURE'''<br />
 ==Overview==
-The 'protein only' hypothesis states that a modified form of normal prion, protein triggers infectious neurodegenerative diseases, such as bovine, spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in, humans. Prion proteins are thought to exist in two different, conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential, for understanding the transition to PrPsc. The nuclear magnetic resonance, (NMR) structure of the autonomously folding PrP domain comprising residues, 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three, alpha-helices. This domain contains most of the point-mutation sites that, have been linked, in human PrP, to the occurrence of familial prion, diseases. The NMR structure shows that these mutations occur within, or, directly adjacent to, regular secondary structures. The presence of a, beta-sheet in PrP(121-231) is in contrast with model predictions of an, all-helical structure of PrPc (ref. 8), and may be important for the, initiation of the transition from PrPc to PrPsc.
+The 'protein only' hypothesis states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain comprising residues 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three alpha-helices. This domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases. The NMR structure shows that these mutations occur within, or directly adjacent to, regular secondary structures. The presence of a beta-sheet in PrP(121-231) is in contrast with model predictions of an all-helical structure of PrPc (ref. 8), and may be important for the initiation of the transition from PrPc to PrPsc.
 ==About this Structure==
-AG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AG2 OCA].
+AG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AG2 OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: prion protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:49:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:07 2008''