Abstract:
:Histone modifications are fundamental to chromatin structure and transcriptional regulation, and are recognized by a limited number of protein folds. Among these folds are PHD fingers, which are present in most chromatin modification complexes. To date, about 15 PHD finger domains have been structurally characterized, whereas hundreds of different sequences have been identified. Consequently, an important open problem is to predict structural features of a PHD finger knowing only its sequence. Here, we classify PHD fingers into different groups based on the analysis of residue-residue co-evolution in their sequences. We measure the degree to which fixing the amino acid type at one position modifies the frequencies of amino acids at other positions. We then detect those position/amino acid combinations, or 'conditions', which have the strongest impact on other sequence positions. Clustering these strong conditions yields four families, providing informative labels for PHD finger sequences. Existing experimental results, as well as docking calculations performed here, reveal that these families indeed show discrepancies at the functional level. Our method should facilitate the functional characterization of new PHD fingers, as well as other protein families, solely based on sequence information.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Slama P,Geman Ddoi
10.1093/nar/gkq947subject
Has Abstractpub_date
2011-03-01 00:00:00pages
1666-79issue
5eissn
0305-1048issn
1362-4962pii
gkq947journal_volume
39pub_type
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journal_title:Nucleic acids research
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