Backbone and side-chain resonance assignments (¹H, ¹⁵N and ¹³C) of the ubiquitin homology domain of mouse BAG-1.
BAG-1, an important regulatory protein associates with several signaling molecules and is capable of suppressing apoptosis. A 97-amino acid segment that includes the ubiquitin homology domain of mouse BAG-1 interacts with the cytoplasmic tail domain of proHB-EGF, and this interaction is likely to have functional significance. Here we report the backbone and side-chain resonance assignments for this 97-amino acid segment of mouse BAG-1. The assignment data has been deposited in the BMRB database under the accession number 18416.
Department of Chemistry, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan, ROC. d9623541@oz.nthu.edu.tw
Hsiao-Wen
HW
Huang
Chin
C
Yu
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011522:Protons; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D014157:Transcription Factors / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry*
C091732:BCL2-associated athanogene 1 protein; D002247:Carbon Isotopes; D004268:DNA-Binding Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D014157:Transcription Factors; D025801:Ubiquitin