Intramolecular cohesion of coils mediated by phenylalanine--glycine motifs in the natively unfolded domain of a nucleoporin.
The nuclear pore complex (NPC) provides the sole aqueous conduit for macromolecular exchange between the nucleus and the cytoplasm of cells. Its diffusion conduit contains a size-selective gate formed by a family of NPC proteins that feature large, natively unfolded domains with phenylalanine-glycin...
Guardado en:
Autores principales: | V V Krishnan, Edmond Y Lau, Justin Yamada, Daniel P Denning, Samir S Patel, Michael E Colvin, Michael F Rexach |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2008
|
Materias: | |
Acceso en línea: | https://doaj.org/article/ceb5cd69ae3b4926bf29d2d110d8e741 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
A switchable self-assembling and disassembling chiral system based on a porphyrin-substituted phenylalanine–phenylalanine motif
por: Georgios Charalambidis, et al.
Publicado: (2016) -
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis
por: Martina K. Ried, et al.
Publicado: (2021) -
Noroviruses Co-opt the Function of Host Proteins VAPA and VAPB for Replication via a Phenylalanine–Phenylalanine-Acidic-Tract-Motif Mimic in Nonstructural Viral Protein NS1/2
por: Broc T. McCune, et al.
Publicado: (2017) -
Nucleoporin Nup155 is part of the p53 network in liver cancer
por: Kerstin Holzer, et al.
Publicado: (2019) -
Nucleoporin TPR is an integral component of the TREX-2 mRNA export pathway
por: Vasilisa Aksenova, et al.
Publicado: (2020)