The ancestral KH peptide at the root of a domain family with three different folds | Zendy

Joana Pereira | Zendy; Andrei N. Lupas | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

The ancestral KH peptide at the root of a domain family with three different folds

Author(s) -

Joana Pereira,

Andrei N. Lupas

Publication year - 2018

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/bty480

Subject(s) - rna , peptide , biology , dna , homology (biology) , computational biology , motif (music) , peptide sequence , genetics , evolutionary biology , gene , biochemistry , physics , acoustics

The direct ancestor of the DNA-protein world of today is considered to have been an RNA-peptide world, in which peptides were co-factors of RNA-mediated catalysis and replication. Evidence for these ancestral peptides, from which folded proteins evolved, can be derived even today from regions of local sequence similarity within globally dissimilar folds. One of these is the 45-residue motif common to both folds of the hnRNP K homology (KH) domain.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research