Cargando…
Comparison of tertiary structures of proteins in protein-protein complexes with unbound forms suggests prevalence of allostery in signalling proteins
BACKGROUND: Most signalling and regulatory proteins participate in transient protein-protein interactions during biological processes. They usually serve as key regulators of various cellular processes and are often stable in both protein-bound and unbound forms. Availability of high-resolution stru...
Autores principales: | Swapna, Lakshmipuram S, Mahajan, Swapnil, de Brevern, Alexandre G, Srinivasan, Narayanaswamy |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427047/ https://www.ncbi.nlm.nih.gov/pubmed/22554255 http://dx.doi.org/10.1186/1472-6807-12-6 |
Ejemplares similares
-
Roles of residues in the interface of transient protein-protein complexes before complexation
por: Swapna, Lakshmipuram S., et al.
Publicado: (2012) -
Extent of Structural Asymmetry in Homodimeric Proteins: Prevalence and Relevance
por: Swapna, Lakshmipuram Seshadri, et al.
Publicado: (2012) -
Identification of Local Conformational Similarity in Structurally Variable Regions of Homologous Proteins Using Protein Blocks
por: Agarwal, Garima, et al.
Publicado: (2011) -
The origins of the evolutionary signal used to predict protein-protein interactions
por: Swapna, Lakshmipuram S, et al.
Publicado: (2012) -
Accommodation of profound sequence differences at the interfaces of eubacterial RNA polymerase multi-protein assembly
por: Swapna, Lakshmipuram Seshadri, et al.
Publicado: (2012)