BRMS151-98 and BRMS151-84 are crystal oligomeric coiled coils with different oligomerization states, which behave as disordered protein fragments in solution.
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Summary
The structural and biophysical features of this region have been studied to further understand the contribution of the N-terminal coiled coil to the biological function of BRMS1 and it is observed that residues 85 to 98 might be important in defining the oligomerization state of the BR MS1 N-TerminalCoiled coil.
- Type
- article
- Published
- 2013-06-26
- Cited by
- 6
- References
- 57
- Access
- Open access
- OpenAlex
- https://openalex.org/W23500495
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:43788891
Keywords
Verb, Argument (complex analysis), Valency, Linguistics, Predicate (mathematical logic)
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Cited by
- Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex
- Falling down: landscape and kinetics of one-dimensional protein folding.
- Mcm10 Self-Association Is Mediated by an N-Terminal Coiled-Coil Domain
- Human COA3 Is an Oligomeric Highly Flexible Protein in Solution.
- The isolated C-terminal nuclear localization sequence of the breast cancer metastasis suppressor 1 is disordered
- A sponge homolog of BRMS1 reveals ancient origin of metastasis-suppressing functions
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