1vig: Difference between revisions

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[[Image:1vig.gif|left|200px]]<br />

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

<applet load="1vig" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1vig" />

'''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES'''<br />

==Overview==

The KH module is a sequence motif found in a number of proteins that are, known to be in close association with RNA. Experimental evidence suggests, a direct involvement of KH in RNA binding. The human FMR1 protein, which, has two KH domains, is associated with fragile X syndrome, the most common, inherited cause of mental retardation. Here we present the, three-dimensional solution structure of the KH module. The domain consists, of a stable beta alpha alpha beta beta alpha fold. On the basis of our, results, we suggest a potential surface for RNA binding centered on the, loop between the first two helices. Substitution of a well-conserved, hydrophobic residue located on the second helix destroys the KH fold; a, mutation of this position in FMR1 leads to an aggravated fragile X, phenotype.

The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three-dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well-conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype.

==About this Structure==

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

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

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Gibson, T.J.]]

[[Category: Gibson, T J.]]

[[Category: Joseph, C.]]

[[Category: Morelli, M.A.C.]]

[[Category: Morelli, M A.C.]]

[[Category: Musco, G.]]

[[Category: Nilges, M.]]

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[[Category: rna-binding protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:39 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1vig.gif|left|200px]]<br />
+[[Image:1vig.gif|left|200px]]<br /><applet load="1vig" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1vig" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1vig" />
 '''NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES'''<br />
 ==Overview==
-The KH module is a sequence motif found in a number of proteins that are, known to be in close association with RNA. Experimental evidence suggests, a direct involvement of KH in RNA binding. The human FMR1 protein, which, has two KH domains, is associated with fragile X syndrome, the most common, inherited cause of mental retardation. Here we present the, three-dimensional solution structure of the KH module. The domain consists, of a stable beta alpha alpha beta beta alpha fold. On the basis of our, results, we suggest a potential surface for RNA binding centered on the, loop between the first two helices. Substitution of a well-conserved, hydrophobic residue located on the second helix destroys the KH fold; a, mutation of this position in FMR1 leads to an aggravated fragile X, phenotype.
+The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three-dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well-conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype.
 ==About this Structure==
-VIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VIG OCA].
+VIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIG OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Gibson, T.J.]]
+[[Category: Gibson, T J.]]
 [[Category: Joseph, C.]]
-[[Category: Morelli, M.A.C.]]
+[[Category: Morelli, M A.C.]]
 [[Category: Musco, G.]]
 [[Category: Nilges, M.]]
@@ Line 23: / Line 22: @@
 [[Category: rna-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:44:02 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:39 2008''