Lim, Jongsoo Hong, Yoon-Hun Lee, Bong-Jin Ahn, Hee-Chul 2024-01-20T17:05:11Z 2024-01-20T17:05:11Z 2021-09-02 2011-04 1874-2718 https://pubs.kist.re.kr/handle/201004/130477 Signal transducing adapter molecule (STAM) forms the endosomal sorting complex required for transport-0 (ESCRT-0) complex with hepatocyte growth factor-regulated substrate (Hrs) to sort the ubiquitinated cargo proteins from the early endosomes to the ESCRT-1 complex. ESCRT-0 complex, STAM and Hrs, contains multiple ubiquitin binding domains, in which STAM has two ubiquitin binding domains, Vps27/Hrs/Stam (VHS) and ubiquitin interacting motif (UIM) at its N-terminus. By the cooperation of the multiple ubiquitin binding domains, the ESCRT-0 complex recognizes poly-ubiquitin, especially Lys63-linked ubiquitin. Here, we report the backbone resonance assignments and the secondary structure of the N-terminal 191 amino acids of the human STAM1 which includes the VHS domain and UIM. The {H-1}-N-15 heteronuclear NOE experiments revealed that an unstructured and flexible loop region connects the VHS domain and UIM. Our work provides the basic information for the further NMR investigation of the interaction between STAM1 and poly-ubiquitin. English SPRINGER PROTEINS Backbone H-1, C-13, and N-15 assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1 Article 10.1007/s12104-010-9265-2 1 BIOMOLECULAR NMR ASSIGNMENTS, v.5, no.1, pp.51 - 54 BIOMOLECULAR NMR ASSIGNMENTS 5 1 51 54 scie scopus 000288076300013 2-s2.0-79952440265 Biophysics Spectroscopy Biophysics Spectroscopy Article PROTEINS Signal transducing adapter molecule Vps27/Hrs/Stam (VHS) Ubiquitin Ubiquitin interacting motif (UIM) Poly-ubiquitin Backbone resonance assignments