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| [[Image:1yjm.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1yjm| PDB=1yjm | SCENE= }} | | {{STRUCTURE_1yjm| PDB=1yjm | SCENE= }} |
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| '''Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.'''
| | ===Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.=== |
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| ==Overview==
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| Mammalian polynucleotide kinase (PNK) is a key component of both the base excision repair (BER) and nonhomologous end-joining (NHEJ) DNA repair pathways. PNK acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. PNK is recruited to repair complexes through interactions between its N-terminal FHA domain and phosphorylated components of either pathway. Here, we describe the crystal structure of intact mammalian PNK and a structure of the PNK FHA bound to a cognate phosphopeptide. The kinase domain has a broad substrate binding pocket, which preferentially recognizes double-stranded substrates with recessed 5' termini. In contrast, the phosphatase domain efficiently dephosphorylates single-stranded 3'-phospho termini as well as double-stranded substrates. The FHA domain is linked to the kinase/phosphatase catalytic domain by a flexible tether, and it exhibits a mode of target selection based on electrostatic complementarity between the binding surface and the phosphothreonine peptide.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15749016}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15749016 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15749016}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Polynucleotide kinase]] | | [[Category: Polynucleotide kinase]] |
| [[Category: Xrcc4 phosphopeptide]] | | [[Category: Xrcc4 phosphopeptide]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:24:13 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:49:25 2008'' |
