Solution structure of the closed conformation of human U2AF65 tandem RRM1 and RRM2 domains

Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF.

STRUCTURE CALCULATION INCLUDED DISTANCE RESTRAINTS BASED ON PARAMAGNETIC RELAXATION ENHANCEMENT DATA FROM SEVEN INDEPENDENT CYSTEINE MUTANTS (N155C, A164C A171C, T209C, D273C, A287C AND A318C) COVALENTLY MODIFIED BY 3-(2-IODOACETAMIDO)-2,2,5,5,TETRAMETHYL-1- PYRROLIDINYLOXY RADICAL (IODOACETAMIDO-PROXYL)
tandem RRM1 and RRM2 domains joined by native linker

Model Of Human U2af65 Tandem Rrm1 And Rrm2 Domains With Eight-Site Uridine Binding

U2 small nuclear RNA auxiliary factor 2 isoform b [Homo sapiens]

U2 small nuclear RNA auxiliary factor 2 [synthetic construct]

unnamed protein product, partial [Tetraodon nigroviridis]

U2 small nuclear ribonucleoprotein auxiliary factor (U2AF) 2 [Mus musculus]

U2 small nuclear RNA auxiliary factor 2 [Homo sapiens]

splicing factor U2AF 65 kDa subunit isoform 2 [Xenopus (Silurana) tropicalis]

splicing factor U2AF 65 kDa subunit isoform b [Homo sapiens]

U2 small nuclear RNA auxiliary factor 2a [Danio rerio]

splicing factor U2AF 65 kDa subunit [Bos taurus]

U2 small nuclear RNA auxiliary factor 2 [Xenopus laevis]

RecName: Full=Splicing factor U2AF 65 kDa subunit; AltName: Full=U2 auxiliary factor 65 kDa subunit; Short=hU2AF(65); Short=hU2

RecName: Full=Splicing factor U2AF 65 kDa subunit; AltName: Full=U2 auxiliary factor 65 kDa subunit; AltName: Full=U2 snRNP aux

TPA: U2 (RNU2) small nuclear RNA auxiliary factor 2 [Bos taurus]

In addition to wildtype protein, NMR data also used seven site-directed cysteine mutants (N155C, A164C, A171C, L187C, A188C, T209C, D273C, S281C, A287C and A318C)

pH [6.5], temp [295], pressure [1], ionStrength [70.0]

Brunger, Adams, Clore, Gros, Nilges and Read