1qgp: Difference between revisions

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==Overview==

Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain, Zalpha. Here we report the solution structure of free Zalpha and map the, interaction surface with Z-DNA, confirming roles previously assigned to, residues by mutagenesis. Comparison with the crystal structure of the, (Zalpha)(2)/Z-DNA complex shows that most Z-DNA contacting residues in, free Zalpha are prepositioned to bind Z-DNA, thus minimizing the entropic, cost of binding. Comparison with homologous, (alpha+beta)helix-turn-helix/B-DNA complexes suggests that binding of, Zalpha to B-DNA is disfavored by steric hindrance, but does not eliminate, the possibility that related domains may bind to both B- and Z-DNA.

Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Zalpha. Here we report the solution structure of free Zalpha and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Zalpha)(2)/Z-DNA complex shows that most Z-DNA contacting residues in free Zalpha are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (alpha+beta)helix-turn-helix/B-DNA complexes suggests that binding of Zalpha to B-DNA is disfavored by steric hindrance, but does not eliminate the possibility that related domains may bind to both B- and Z-DNA.

==Disease==

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[[Category: Schade, M.]]

[[Category: Schmieder, P.]]

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

[[Category: Turner, C J.]]

[[Category: adar1]]

[[Category: helix- turn-helix]]

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[[Category: z-dna recognition]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:21 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain, Zalpha. Here we report the solution structure of free Zalpha and map the, interaction surface with Z-DNA, confirming roles previously assigned to, residues by mutagenesis. Comparison with the crystal structure of the, (Zalpha)(2)/Z-DNA complex shows that most Z-DNA contacting residues in, free Zalpha are prepositioned to bind Z-DNA, thus minimizing the entropic, cost of binding. Comparison with homologous, (alpha+beta)helix-turn-helix/B-DNA complexes suggests that binding of, Zalpha to B-DNA is disfavored by steric hindrance, but does not eliminate, the possibility that related domains may bind to both B- and Z-DNA.
+Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Zalpha. Here we report the solution structure of free Zalpha and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Zalpha)(2)/Z-DNA complex shows that most Z-DNA contacting residues in free Zalpha are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (alpha+beta)helix-turn-helix/B-DNA complexes suggests that binding of Zalpha to B-DNA is disfavored by steric hindrance, but does not eliminate the possibility that related domains may bind to both B- and Z-DNA.
 ==Disease==
@@ Line 23: / Line 23: @@
 [[Category: Schade, M.]]
 [[Category: Schmieder, P.]]
-[[Category: Turner, C.J.]]
+[[Category: Turner, C J.]]
 [[Category: adar1]]
 [[Category: helix- turn-helix]]
@@ Line 30: / Line 30: @@
 [[Category: z-dna recognition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:44:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:21 2008''