Ontology highlight
ABSTRACT:
SUBMITTER: Hwang KJ
PROVIDER: S-EPMC1783391 | biostudies-literature | 2007 Jan
REPOSITORIES: biostudies-literature
Hwang Kae-Jung KJ Mahmoodian Fatemeh F Ferretti James A JA Korn Edward D ED Gruschus James M JM
Proceedings of the National Academy of Sciences of the United States of America 20070110 3
The 466-aa tail of the heavy chain of Acanthamoeba myosin IC (AMIC) comprises an N-terminal 220-residue basic region (BR) followed by a 56-residue Gly/Pro/Ala-rich region (GPA1), a 55-residue Src homology 3 (SH3) domain, and a C-terminal 135-residue Gly/Pro/Ala-rich region (GPA2). Cryo-electron microscopy of AMIC had shown previously that the AMIC tail is folded back on itself, suggesting the possibility of interactions between its N- and C-terminal regions. We now show specific differences betw ...[more]