6bzm
From Proteopedia
GFGNFGTS from low-complexity/FG repeat domain of Nup98, residues 116-123
Structural highlights
Disease[NUP98_HUMAN] Note=A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23. Note=A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1. Note=A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1. Note=A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1. Note=A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4. Function[NUP98_HUMAN] Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The FG repeat domains in Nup98 have a direct role in the transport. Publication Abstract from PubMedSubcellular membraneless assemblies are a reinvigorated area of study in biology, with spirited scientific discussions on the forces between the low-complexity protein domains within these assemblies. To illuminate these forces, we determined the atomic structures of five segments from protein low-complexity domains associated with membraneless assemblies. Their common structural feature is the stacking of segments into kinked beta sheets that pair into protofilaments. Unlike steric zippers of amyloid fibrils, the kinked sheets interact weakly through polar atoms and aromatic side chains. By computationally threading the human proteome on our kinked structures, we identified hundreds of low-complexity segments potentially capable of forming such interactions. These segments are found in proteins as diverse as RNA binders, nuclear pore proteins, and keratins, which are known to form networks and localize to membraneless assemblies. Atomic structures of low-complexity protein segments reveal kinked beta sheets that assemble networks.,Hughes MP, Sawaya MR, Boyer DR, Goldschmidt L, Rodriguez JA, Cascio D, Chong L, Gonen T, Eisenberg DS Science. 2018 Feb 9;359(6376):698-701. doi: 10.1126/science.aan6398. PMID:29439243[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Cascio, D | Chong, L | Eisenberg, D S | Gonen, T | Hughes, M P | Rodriguez, J A | Sawaya, M R | Amyloid | Fg repeat | Lark | Low-complexity | Protein fibril | Reversible-amyloid
