2spc: Difference between revisions

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[[Image:2spc.jpg|left|200px]]<br /><applet load="2spc" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2spc.jpg|left|200px]]<br /><applet load="2spc" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2spc, resolution 1.8Å" />

'''CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN'''<br />

==Overview==

The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient, cellular meshworks by cross-linking actin filaments. The structure of one, of the repetitive segments of alpha-spectrin was determined at a 1.8, angstrom resolution. A segment consists of a three-helix bundle. A model, of the interface between two tandem segments suggests that hydrophobic, interactions between segments may constrain intersegment flexibility. The, helix side chain interactions explain how mutations that are known to, produce hemolytic anemias disrupt spectrin associations that sustain the, integrity of the erythrocyte membrane.

The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.

==About this Structure==

2SPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2SPC OCA].

2SPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SPC OCA].

==Reference==

Line 15:

[[Category: Branton, D.]]

[[Category: Cronin, T.]]

[[Category: Harrison, S.C.]]

[[Category: Harrison, S C.]]

[[Category: Viel, A.]]

[[Category: Winograd, E.]]

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[[Category: cytoskeleton]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 14:02:~~44 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:23 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2spc.jpg|left|200px]]<br /><applet load="2spc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2spc.jpg|left|200px]]<br /><applet load="2spc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2spc, resolution 1.8&Aring;" />
 '''CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN'''<br />
 ==Overview==
-The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient, cellular meshworks by cross-linking actin filaments. The structure of one, of the repetitive segments of alpha-spectrin was determined at a 1.8, angstrom resolution. A segment consists of a three-helix bundle. A model, of the interface between two tandem segments suggests that hydrophobic, interactions between segments may constrain intersegment flexibility. The, helix side chain interactions explain how mutations that are known to, produce hemolytic anemias disrupt spectrin associations that sustain the, integrity of the erythrocyte membrane.
+The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.
 ==About this Structure==
-SPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2SPC OCA].
+SPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SPC OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Branton, D.]]
 [[Category: Cronin, T.]]
-[[Category: Harrison, S.C.]]
+[[Category: Harrison, S C.]]
 [[Category: Viel, A.]]
 [[Category: Winograd, E.]]
@@ Line 21: / Line 21: @@
 [[Category: cytoskeleton]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 14:02:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:23 2008''