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-[[Image:1wtb.gif|left|200px]]<br />
+[[Image:1wtb.gif|left|200px]]<br /><applet load="1wtb" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1wtb" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1wtb" />
 '''Complex structure of the C-terminal RNA-binding domain of hnRNP D (AUF1) with telomere DNA'''<br />
 ==Overview==
-Heterogeneous nuclear ribonucleoprotein D, also known as AUF1, has two, DNA/RNA-binding domains, each of which can specifically bind to, single-stranded d(TTAGGG)n, the human telomeric repeat. Here, the, structure of the C-terminal-binding domain (BD2) complexed with, single-stranded d(TTAGGG) determined by NMR is presented. The structure, has revealed that each residue of the d(TAG) segment is recognized by BD2, in a base-specific manner. The interactions deduced from the structure, have been confirmed by gel retardation experiments with mutant BD2 and, DNA. It is known that single-stranded DNA with the telomeric repeat tends, to form a quadruplex and that the quadruplex has an inhibitory effect on, telomere elongation by telomerase. This time it is revealed that BD2, unfolds the quadruplex of such DNA upon binding. Moreover, the effect of, BD2 on the elongation by telomerase was examined in vitro. These results, suggest the possible involvement of heterogeneous nuclear, ribonucleoprotein D in maintenance of the telomere 3'-overhang either, through protection of a single-stranded DNA or destabilization of the, potentially deleterious quadruplex structure for the elongation by, telomerase.
+Heterogeneous nuclear ribonucleoprotein D, also known as AUF1, has two DNA/RNA-binding domains, each of which can specifically bind to single-stranded d(TTAGGG)n, the human telomeric repeat. Here, the structure of the C-terminal-binding domain (BD2) complexed with single-stranded d(TTAGGG) determined by NMR is presented. The structure has revealed that each residue of the d(TAG) segment is recognized by BD2 in a base-specific manner. The interactions deduced from the structure have been confirmed by gel retardation experiments with mutant BD2 and DNA. It is known that single-stranded DNA with the telomeric repeat tends to form a quadruplex and that the quadruplex has an inhibitory effect on telomere elongation by telomerase. This time it is revealed that BD2 unfolds the quadruplex of such DNA upon binding. Moreover, the effect of BD2 on the elongation by telomerase was examined in vitro. These results suggest the possible involvement of heterogeneous nuclear ribonucleoprotein D in maintenance of the telomere 3'-overhang either through protection of a single-stranded DNA or destabilization of the potentially deleterious quadruplex structure for the elongation by telomerase.
 ==About this Structure==
-WTB 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=1WTB OCA].
+WTB 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=1WTB OCA].
 ==Reference==
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 [[Category: telomere]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:54:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:54 2008''