2jm3: Difference between revisions

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==Overview==

The THAP (Thanatos-associated protein) domain is a recently discovered, zinc-binding domain found in proteins involved in transcriptional, regulation, cell-cycle control, apoptosis and chromatin modification. It, contains a single zinc atom ligated by cysteine and histidine residues, within a Cys-X(2-4)-Cys-X(35-53)-Cys-X(2)-His consensus. We have, determined the NMR solution structure of the THAP domain from, Caenorhabditis elegans C-terminal binding protein (CtBP) and show that it, adopts a fold containing a treble clef motif, bearing similarity to the, zinc finger-associated domain (ZAD) from Drosophila Grauzone. The CtBP, THAP domain contains a large, positively charged surface patch and we, demonstrate that this domain can bind to double-stranded DNA in an, electrophoretic mobility-shift assay. These data, together with existing, reports, indicate that THAP domains might exhibit a functional diversity, similar to that observed for classical and GATA-type zinc fingers.

The THAP (Thanatos-associated protein) domain is a recently discovered zinc-binding domain found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. It contains a single zinc atom ligated by cysteine and histidine residues within a Cys-X(2-4)-Cys-X(35-53)-Cys-X(2)-His consensus. We have determined the NMR solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP) and show that it adopts a fold containing a treble clef motif, bearing similarity to the zinc finger-associated domain (ZAD) from Drosophila Grauzone. The CtBP THAP domain contains a large, positively charged surface patch and we demonstrate that this domain can bind to double-stranded DNA in an electrophoretic mobility-shift assay. These data, together with existing reports, indicate that THAP domains might exhibit a functional diversity similar to that observed for classical and GATA-type zinc fingers.

==About this Structure==

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[[Category: Single protein]]

[[Category: Crossley, M.]]

[[Category: Liew, C.K.]]

[[Category: Liew, C K.]]

[[Category: Mackay, J.P.]]

[[Category: Mackay, J P.]]

[[Category: Nicholas, H.R.]]

[[Category: Nicholas, H R.]]

[[Category: ZN]]

[[Category: domain]]

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[[Category: zinc finger]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The THAP (Thanatos-associated protein) domain is a recently discovered, zinc-binding domain found in proteins involved in transcriptional, regulation, cell-cycle control, apoptosis and chromatin modification. It, contains a single zinc atom ligated by cysteine and histidine residues, within a Cys-X(2-4)-Cys-X(35-53)-Cys-X(2)-His consensus. We have, determined the NMR solution structure of the THAP domain from, Caenorhabditis elegans C-terminal binding protein (CtBP) and show that it, adopts a fold containing a treble clef motif, bearing similarity to the, zinc finger-associated domain (ZAD) from Drosophila Grauzone. The CtBP, THAP domain contains a large, positively charged surface patch and we, demonstrate that this domain can bind to double-stranded DNA in an, electrophoretic mobility-shift assay. These data, together with existing, reports, indicate that THAP domains might exhibit a functional diversity, similar to that observed for classical and GATA-type zinc fingers.
+The THAP (Thanatos-associated protein) domain is a recently discovered zinc-binding domain found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. It contains a single zinc atom ligated by cysteine and histidine residues within a Cys-X(2-4)-Cys-X(35-53)-Cys-X(2)-His consensus. We have determined the NMR solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP) and show that it adopts a fold containing a treble clef motif, bearing similarity to the zinc finger-associated domain (ZAD) from Drosophila Grauzone. The CtBP THAP domain contains a large, positively charged surface patch and we demonstrate that this domain can bind to double-stranded DNA in an electrophoretic mobility-shift assay. These data, together with existing reports, indicate that THAP domains might exhibit a functional diversity similar to that observed for classical and GATA-type zinc fingers.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Crossley, M.]]
-[[Category: Liew, C.K.]]
+[[Category: Liew, C K.]]
-[[Category: Mackay, J.P.]]
+[[Category: Mackay, J P.]]
-[[Category: Nicholas, H.R.]]
+[[Category: Nicholas, H R.]]
 [[Category: ZN]]
 [[Category: domain]]
@@ Line 22: / Line 22: @@
 [[Category: zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:53:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:03:53 2008''