Mutation Information
Mutation Site
|
D150A |
Mutation Type
|
Amino acid level |
Gene/Protein/Region Type
|
LMP1 |
Literature Information
PubMed PMID
|
21560118
|
Published Year
|
2011 |
Journal
|
Biopolymers |
Title
|
Transmembrane peptides used to investigate the homo-oligomeric interface and binding hotspot of latent membrane protein 1. |
Author
|
Sammond DW,Joce C,Takeshita R,McQuate SE,Ghosh N,Martin JM,Yin H |
Evidence
|
Replacement of this aspartic acid residue with alanine disrupts TM5 self-association in detergent micelles and bacterial cell membranes. A full length LMP-1 variant harboring the D150A substitution is deficient in NFkappaB activation, supporting the key role of the fifth transmembrane helix in constitutive activation of signaling by this oncoprotein.
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