2dut: Difference between revisions

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

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

caption="2dut, resolution 3.0Å" />

'''Crystal structure of a M-loop deletion variant of MENT in the native conformation'''<br />

==Overview==

Most serpins are associated with protease inhibition, and their ability to, form loop-sheet polymers is linked to conformational disease and the human, serpinopathies. Here we describe the structural and functional dissection, of how a unique serpin, the non-histone architectural protein, MENT, (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT, contains at least two distinct DNA-binding sites, consistent with its, simultaneous binding to the two closely juxtaposed linker DNA segments on, a nucleosome. Remarkably, our studies suggest that the reactive centre, loop, a region of the MENT molecule essential for chromatin bridging in, vivo and in vitro, is able to mediate formation of a loop-sheet oligomer., These data provide mechanistic insight into chromatin compaction by a, non-histone architectural protein and suggest how the structural, plasticity of serpins has adapted to mediate physiological, rather than, pathogenic, loop-sheet linkages.

Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages.

==About this Structure==

2DUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure ~~superseeds~~ the now removed PDB entry 2H4S. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2DUT OCA].

2DUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry 2H4S. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUT OCA].

==Reference==

Line 13:

[[Category: Gallus gallus]]

[[Category: Single protein]]

[[Category: Buckle, A.M.]]

[[Category: Buckle, A M.]]

[[Category: Irving, J.A.]]

[[Category: Irving, J A.]]

[[Category: McGowan, S.]]

[[Category: Whisstock, J.C.]]

[[Category: Whisstock, J C.]]

[[Category: serine protease inhibitor]]

[[Category: serpin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 25 08~~:55:~~11 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:53 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2dut.gif|left|200px]]<br /><applet load="2dut" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2dut.gif|left|200px]]<br /><applet load="2dut" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2dut, resolution 3.0&Aring;" />
 '''Crystal structure of a M-loop deletion variant of MENT in the native conformation'''<br />
 ==Overview==
-Most serpins are associated with protease inhibition, and their ability to, form loop-sheet polymers is linked to conformational disease and the human, serpinopathies. Here we describe the structural and functional dissection, of how a unique serpin, the non-histone architectural protein, MENT, (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT, contains at least two distinct DNA-binding sites, consistent with its, simultaneous binding to the two closely juxtaposed linker DNA segments on, a nucleosome. Remarkably, our studies suggest that the reactive centre, loop, a region of the MENT molecule essential for chromatin bridging in, vivo and in vitro, is able to mediate formation of a loop-sheet oligomer., These data provide mechanistic insight into chromatin compaction by a, non-histone architectural protein and suggest how the structural, plasticity of serpins has adapted to mediate physiological, rather than, pathogenic, loop-sheet linkages.
+Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages.
 ==About this Structure==
-DUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure superseeds the now removed PDB entry 2H4S. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DUT OCA].
+DUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry 2H4S. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUT OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Gallus gallus]]
 [[Category: Single protein]]
-[[Category: Buckle, A.M.]]
+[[Category: Buckle, A M.]]
-[[Category: Irving, J.A.]]
+[[Category: Irving, J A.]]
 [[Category: McGowan, S.]]
-[[Category: Whisstock, J.C.]]
+[[Category: Whisstock, J C.]]
 [[Category: serine protease inhibitor]]
 [[Category: serpin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 08:55:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:53 2008''