1dpu: Difference between revisions

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

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

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

caption="1dpu" />

'''SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)'''<br />

==Overview==

Replication protein A (RPA), the nuclear ssDNA-binding protein in, eukaryotes, is essential to DNA replication, recombination, and repair. We, have shown that a globular domain at the C terminus of subunit RPA32, contains a specific surface that interacts in a similar manner with the, DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which, functions in a different repair pathway. NMR structures of the RPA32, domain, free and in complex with the minimal interaction domain of UNG2, were determined, defining a common structural basis for linking RPA to the, nucleotide excision, base excision, and recombinational pathways of, repairing damaged DNA. Our findings support a hand-off model for the, assembly and coordination of different components of the DNA repair, machinery.

Replication protein A (RPA), the nuclear ssDNA-binding protein in eukaryotes, is essential to DNA replication, recombination, and repair. We have shown that a globular domain at the C terminus of subunit RPA32 contains a specific surface that interacts in a similar manner with the DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which functions in a different repair pathway. NMR structures of the RPA32 domain, free and in complex with the minimal interaction domain of UNG2, were determined, defining a common structural basis for linking RPA to the nucleotide excision, base excision, and recombinational pathways of repairing damaged DNA. Our findings support a hand-off model for the assembly and coordination of different components of the DNA repair machinery.

==Disease==

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==About this Structure==

1DPU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DPU OCA].

1DPU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DPU OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Chazin, W.J.]]

[[Category: Chazin, W J.]]

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

[[Category: Edwards, A M.]]

[[Category: Mer, G.]]

[[Category: dna repair]]

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[[Category: protein-peptide complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:34:~~52 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:12 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dpu.gif|left|200px]]<br />
+[[Image:1dpu.gif|left|200px]]<br /><applet load="1dpu" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1dpu" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1dpu" />
 '''SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)'''<br />
 ==Overview==
-Replication protein A (RPA), the nuclear ssDNA-binding protein in, eukaryotes, is essential to DNA replication, recombination, and repair. We, have shown that a globular domain at the C terminus of subunit RPA32, contains a specific surface that interacts in a similar manner with the, DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which, functions in a different repair pathway. NMR structures of the RPA32, domain, free and in complex with the minimal interaction domain of UNG2, were determined, defining a common structural basis for linking RPA to the, nucleotide excision, base excision, and recombinational pathways of, repairing damaged DNA. Our findings support a hand-off model for the, assembly and coordination of different components of the DNA repair, machinery.
+Replication protein A (RPA), the nuclear ssDNA-binding protein in eukaryotes, is essential to DNA replication, recombination, and repair. We have shown that a globular domain at the C terminus of subunit RPA32 contains a specific surface that interacts in a similar manner with the DNA repair enzyme UNG2 and repair factors XPA and RAD52, each of which functions in a different repair pathway. NMR structures of the RPA32 domain, free and in complex with the minimal interaction domain of UNG2, were determined, defining a common structural basis for linking RPA to the nucleotide excision, base excision, and recombinational pathways of repairing damaged DNA. Our findings support a hand-off model for the assembly and coordination of different components of the DNA repair machinery.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-DPU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DPU OCA].
+DPU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DPU OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Chazin, W.J.]]
+[[Category: Chazin, W J.]]
-[[Category: Edwards, A.M.]]
+[[Category: Edwards, A M.]]
 [[Category: Mer, G.]]
 [[Category: dna repair]]
@@ Line 24: / Line 23: @@
 [[Category: protein-peptide complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:34:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:12 2008''