Ontology highlight
ABSTRACT:
SUBMITTER: Jogl G
PROVIDER: S-EPMC126298 | biostudies-literature | 2002 Sep
REPOSITORIES: biostudies-literature
Jogl Gerwald G Shen Yang Y Gebauer Damara D Li Jiang J Wiegmann Katja K Kashkar Hamid H Krönke Martin M Tong Liang L
The EMBO journal 20020901 18
The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary st ...[more]