This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1akz
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1akz.png|left|200px]] | ||
| - | |||
{{STRUCTURE_1akz| PDB=1akz | SCENE= }} | {{STRUCTURE_1akz| PDB=1akz | SCENE= }} | ||
| - | |||
===HUMAN URACIL-DNA GLYCOSYLASE=== | ===HUMAN URACIL-DNA GLYCOSYLASE=== | ||
| + | {{ABSTRACT_PUBMED_9724657}} | ||
| - | + | ==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> | ||
| + | |||
| + | ==Function== | ||
| + | [[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== | ||
| Line 14: | Line 16: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:009724657</ref><ref group="xtra">PMID:011679752</ref><ref group="xtra">PMID:016411755</ref><references group="xtra"/> | + | <ref group="xtra">PMID:009724657</ref><ref group="xtra">PMID:011679752</ref><ref group="xtra">PMID:016411755</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mol, C D.]] | [[Category: Mol, C D.]] | ||
Revision as of 01:59, 25 March 2013
Contents |
HUMAN URACIL-DNA GLYCOSYLASE
Template:ABSTRACT PUBMED 9724657
Disease
[UNG_HUMAN] Defects in UNG are a cause of immunodeficiency with hyper-IgM type 5 (HIGM5) [MIM: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.[1][2]
Function
[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
1akz is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Parikh SS, Mol CD, Slupphaug G, Bharati S, Krokan HE, Tainer JA. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 1998 Sep 1;17(17):5214-26. PMID:9724657 doi:10.1093/emboj/17.17.5214
- Leiros I, Lanes O, Sundheim O, Helland R, Smalas AO, Willassen NP. Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua). Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1706-8. Epub 2001, Oct 25. PMID:11679752
- Qin J, Chai G, Brewer JM, Lovelace LL, Lebioda L. Fluoride inhibition of enolase: crystal structure and thermodynamics. Biochemistry. 2006 Jan 24;45(3):793-800. PMID:16411755 doi:10.1021/bi051558s
- ↑ Imai K, Slupphaug G, Lee WI, Revy P, Nonoyama S, Catalan N, Yel L, Forveille M, Kavli B, Krokan HE, Ochs HD, Fischer A, Durandy A. Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination. Nat Immunol. 2003 Oct;4(10):1023-8. Epub 2003 Sep 7. PMID:12958596 doi:http://dx.doi.org/10.1038/ni974
- ↑ Kavli B, Andersen S, Otterlei M, Liabakk NB, Imai K, Fischer A, Durandy A, Krokan HE, Slupphaug G. B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil. J Exp Med. 2005 Jun 20;201(12):2011-21. PMID:15967827 doi:10.1084/jem.20050042
