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[[Image:1dpu.png|left|200px]]
{{STRUCTURE_1dpu|  PDB=1dpu  |  SCENE=  }}  
{{STRUCTURE_1dpu|  PDB=1dpu  |  SCENE=  }}  
===SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)===
{{ABSTRACT_PUBMED_11081631}}


===SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN RPA32 COMPLEXED WITH UNG2(73-88)===
==Disease==
[[http://www.uniprot.org/uniprot/UNG_HUMAN UNG_HUMAN]] Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5) [MIM:[http://omim.org/entry/608106 608106]]. A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.<ref>PMID:12958596</ref><ref>PMID:15967827</ref>


{{ABSTRACT_PUBMED_11081631}}
==Function==
[[http://www.uniprot.org/uniprot/RFA2_HUMAN RFA2_HUMAN]] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.<ref>PMID:15205463</ref><ref>PMID:19116208</ref><ref>PMID:19996105</ref><ref>PMID:20154705</ref>  Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:15205463</ref><ref>PMID:19116208</ref><ref>PMID:19996105</ref><ref>PMID:20154705</ref> [[http://www.uniprot.org/uniprot/UNG_HUMAN UNG_HUMAN]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:011081631</ref><ref group="xtra">PMID:019621872</ref><references group="xtra"/>
<ref group="xtra">PMID:011081631</ref><ref group="xtra">PMID:019621872</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chazin, W J.]]
[[Category: Chazin, W J.]]