2M85
PHD Domain from Human SHPRH
Summary for 2M85
| Entry DOI | 10.2210/pdb2m85/pdb |
| Related | 1WEP 1X4I 1XWH 2FUI 2JMI 2K16 2K1J 2KKG 2RSD 2VPD |
| NMR Information | BMRB: 19229 |
| Descriptor | E3 ubiquitin-protein ligase SHPRH, ZINC ION (2 entities in total) |
| Functional Keywords | shprh, snf2, histone linker, phd finger, ring finger, helicase, hydrolase, ligase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8720.73 |
| Authors | Machado, L.E.S.F.,Pustovalova, Y.,Pozhidaeva, A.,Almeida, F.C.L.,Bezsonova, I.,Korzhnev, D.M. (deposition date: 2013-05-07, release date: 2013-08-14, Last modification date: 2024-05-01) |
| Primary citation | Machado, L.E.,Pustovalova, Y.,Kile, A.C.,Pozhidaeva, A.,Cimprich, K.A.,Almeida, F.C.,Bezsonova, I.,Korzhnev, D.M. PHD domain from human SHPRH. J.Biomol.Nmr, 56:393-399, 2013 Cited by PubMed Abstract: SHPRH (NF2, istone linker, HD, ING, elicase) is a SWI2/SNF2-family ATP-dependent chromatin remodeling factor, and one of E3 ubiquitin ligases responsible for Ubc13-Mms2-dependent K63 poly-ubiquitination of PCNA (roliferating ell uclear ntigen) that promotes error-free DNA damage tolerance in eukaryotes. In contrast to its functional homologues, Rad5 and human HLTF (elicase ike ranscription actor), SHPRH contains a PHD (lant omeoomain) finger embedded in the ‘minor’ insert region of the core helicase-like domain. PHD fingers are often found in proteins involved in chromatin remodeling and transcription regulation, and are generally considered as ‘readers’ of methylation state of histone tails, primarily the lysine 4 (K4) residue of histone H3 (H3K4). Here we report the solution NMR structure of the SHPRH PHD domain and investigate whether this domain is capable of recognizing H3K4 modifications. The domain adopts a canonical PHD-finger fold with a central two-stranded anti-parallel β-sheet flanked on both sides by the two interleaved zinc-binding sites. Despite the presence of a subset of aromatic residues characteristic for PHD-fingers that preferentially bind methylated H3K4, NMR titration experiments reveal that SHPRH PHD does not specifically interact with the H3-derived peptides irrespective of K4 methylation. This result suggests that the SHPRH PHD domain might have evolved a different function other than recognizing histone modifications. PubMed: 23907177DOI: 10.1007/s10858-013-9758-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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