A Structurally-Validated Multiple Sequence Alignment of 497 Human Protein Kinase Domains.

ABSTRACT: Studies on the structures and functions of individual kinases have been used to understand the biological properties of other kinases that do not yet have experimental structures. The key factor in accurate inference by homology is an accurate sequence alignment. We present a parsimonious, structure-based multiple sequence alignment (MSA) of 497 human protein kinase domains excluding atypical kinases. The alignment is arranged in 17 blocks of conserved regions and unaligned blocks in between that contain insertions of varying lengths present in only a subset of kinases. The aligned blocks contain well-conserved elements of secondary structure and well-known functional motifs, such as the DFG and HRD motifs. From pairwise, all-against-all alignment of 272 human kinase structures, we estimat

SUBMITTER: Modi V 

PROVIDER: S-EPMC6930252 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature