1t94

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(New page: 200px<br /> <applet load="1t94" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t94, resolution 2.40&Aring;" /> '''Crystal structure o...)
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[[Image:1t94.gif|left|200px]]<br /><applet load="1t94" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1t94" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1t94, resolution 2.40&Aring;" />
caption="1t94, resolution 2.40&Aring;" />
'''Crystal structure of the catalytic core of human DNA polymerase kappa'''<br />
'''Crystal structure of the catalytic core of human DNA polymerase kappa'''<br />
==Overview==
==Overview==
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We present the crystal structure of the catalytic core of human DNA, polymerase kappa (hPolkappa), the first structure of a human Y-family, polymerase. hPolkappa is implicated in the proficient extension of, mispaired primer termini on undamaged DNAs, and in the extension step of, lesion bypass. The structure reveals a stubby "fingers" subdomain, which, despite its small size appears to be tightly restrained with respect to a, putative templating base. The structure also reveals a novel "thumb", subdomain that provides a basis for the importance of the N-terminal, extension unique to hPolkappa. And, most surprisingly, the structure, reveals the polymerase-associated domain (PAD) juxtaposed on the dorsal, side of the "palm" subdomain, as opposed to the fingers subdomain., Together, these properties suggest that the hPolkappa active site is, constrained at the site of the templating base and incoming nucleotide, but the polymerase is less constrained following translocation of the, lesion.
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We present the crystal structure of the catalytic core of human DNA polymerase kappa (hPolkappa), the first structure of a human Y-family polymerase. hPolkappa is implicated in the proficient extension of mispaired primer termini on undamaged DNAs, and in the extension step of lesion bypass. The structure reveals a stubby "fingers" subdomain, which despite its small size appears to be tightly restrained with respect to a putative templating base. The structure also reveals a novel "thumb" subdomain that provides a basis for the importance of the N-terminal extension unique to hPolkappa. And, most surprisingly, the structure reveals the polymerase-associated domain (PAD) juxtaposed on the dorsal side of the "palm" subdomain, as opposed to the fingers subdomain. Together, these properties suggest that the hPolkappa active site is constrained at the site of the templating base and incoming nucleotide, but the polymerase is less constrained following translocation of the lesion.
==About this Structure==
==About this Structure==
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1T94 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=1T94 OCA].
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1T94 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=1T94 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Aggarwal, A K.]]
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[[Category: Edwards, T.A.]]
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[[Category: Edwards, T A.]]
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[[Category: Johnson, R.E.]]
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[[Category: Johnson, R E.]]
[[Category: Prakash, L.]]
[[Category: Prakash, L.]]
[[Category: Prakash, S.]]
[[Category: Prakash, S.]]
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[[Category: Uljon, S.N.]]
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[[Category: Uljon, S N.]]
[[Category: replication; dna repair; y-family dna polymerase; translesion dna synthesis; lesion bypass]]
[[Category: replication; dna repair; y-family dna polymerase; translesion dna synthesis; lesion bypass]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:22:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:13 2008''

Revision as of 13:11, 21 February 2008


1t94, resolution 2.40Å

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Crystal structure of the catalytic core of human DNA polymerase kappa

Overview

We present the crystal structure of the catalytic core of human DNA polymerase kappa (hPolkappa), the first structure of a human Y-family polymerase. hPolkappa is implicated in the proficient extension of mispaired primer termini on undamaged DNAs, and in the extension step of lesion bypass. The structure reveals a stubby "fingers" subdomain, which despite its small size appears to be tightly restrained with respect to a putative templating base. The structure also reveals a novel "thumb" subdomain that provides a basis for the importance of the N-terminal extension unique to hPolkappa. And, most surprisingly, the structure reveals the polymerase-associated domain (PAD) juxtaposed on the dorsal side of the "palm" subdomain, as opposed to the fingers subdomain. Together, these properties suggest that the hPolkappa active site is constrained at the site of the templating base and incoming nucleotide, but the polymerase is less constrained following translocation of the lesion.

About this Structure

1T94 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic core of human DNA polymerase kappa., Uljon SN, Johnson RE, Edwards TA, Prakash S, Prakash L, Aggarwal AK, Structure. 2004 Aug;12(8):1395-404. PMID:15296733

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