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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0037949,
umls-concept:C0162807,
umls-concept:C0205372,
umls-concept:C0231881,
umls-concept:C0337611,
umls-concept:C0525039,
umls-concept:C0680730,
umls-concept:C1148554,
umls-concept:C1514562,
umls-concept:C1516050,
umls-concept:C1524075,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
32
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pubmed:dateCreated |
1994-9-29
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pubmed:abstractText |
DNA polymerase beta consists of an N-terminal single-stranded DNA binding domain and a C-terminal catalytic domain separable by mild proteolysis [Kumar et al. (1990) J. Biol. Chem. 265, 2124-2131]. The N-terminal domain participates in template and gapped DNA recognition and contributes significantly to catalysis. The secondary structure and tertiary contacts within the cloned N-terminal domain (residues 2-87) of mammalian DNA polymerase beta have been determined using multidimensional NMR. Assignments of backbone 1H, 15N, and 13C resonances and side chain 1H and 13C resonances have been obtained from double- and triple-resonance 3D NMR experiments. The 13C-edited TOCSY experiment has allowed nearly complete assignments of 1H and 13C resonances within side chains. The 13C-edited NOESY experiment has been used for determination of medium- and long-range NOEs and a determination of tertiary contacts. The N-terminal domain is found to consist of four helices, helix-1 (15-26), helix-2 (36-47), helix-3 (56-61), and helix-4 (69-78), which on the basis of long-range NOEs are tightly packed of form a hydrophobic core. The remainder of the domain consists of two turns (48-51 and 62-65), an omega-type loop (27-35), and extended structure. The aromatic side chains of Y36, Y39, Y49, and F76 display tertiary contacts indicative of at least partial hydrophobic packing. The S30 and H34 residues which cross-link to single-stranded DNA [Prasad et al. (1993) J. Biol. Chem. 268, 15906-15911] are contained within the K27-K35 loop.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
33
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9537-45
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8068628-Amino Acid Sequence,
pubmed-meshheading:8068628-Animals,
pubmed-meshheading:8068628-DNA Nucleotidylexotransferase,
pubmed-meshheading:8068628-DNA Polymerase I,
pubmed-meshheading:8068628-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8068628-Models, Molecular,
pubmed-meshheading:8068628-Molecular Sequence Data,
pubmed-meshheading:8068628-Peptide Fragments,
pubmed-meshheading:8068628-Protein Structure, Secondary,
pubmed-meshheading:8068628-Protein Structure, Tertiary,
pubmed-meshheading:8068628-Rats,
pubmed-meshheading:8068628-Recombinant Proteins,
pubmed-meshheading:8068628-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
Assignments of 1H, 15N, and 13C resonances for the backbone and side chains of the N-terminal domain of DNA polymerase beta. Determination of the secondary structure and tertiary contacts.
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pubmed:affiliation |
Department of Chemistry, University of Wisconsin-Milwaukee 53211.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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