+
Open data
-
Basic information
Entry | Database: PDB / ID: 2sxl | ||||||
---|---|---|---|---|---|---|---|
Title | SEX-LETHAL RBD1, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
![]() | SEX-LETHAL PROTEIN | ||||||
![]() | RNA-BINDING DOMAIN / ALTERNATIVE SPLICING / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | ![]() sex determination, primary response to X:A ratio / germarium-derived cystoblast division / epithelium regeneration / female sex determination / somatic sex determination / female germ-line sex determination / oocyte differentiation / imaginal disc growth / negative regulation of RNA export from nucleus / regulation of stem cell division ...sex determination, primary response to X:A ratio / germarium-derived cystoblast division / epithelium regeneration / female sex determination / somatic sex determination / female germ-line sex determination / oocyte differentiation / imaginal disc growth / negative regulation of RNA export from nucleus / regulation of stem cell division / sex determination / poly-pyrimidine tract binding / sex-chromosome dosage compensation / sex differentiation / alternative mRNA splicing, via spliceosome / negative regulation of receptor signaling pathway via JAK-STAT / poly(A) binding / pre-mRNA binding / positive regulation of smoothened signaling pathway / regulation of mRNA splicing, via spliceosome / reciprocal meiotic recombination / poly(U) RNA binding / oogenesis / regulation of alternative mRNA splicing, via spliceosome / negative regulation of mRNA splicing, via spliceosome / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / mRNA 3'-UTR binding / mRNA 5'-UTR binding / protein stabilization / negative regulation of translation / ribonucleoprotein complex / mRNA binding / protein-containing complex / RNA binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY, SIMULATED ANNEALING METHOD | ||||||
![]() | Inoue, M. / Muto, Y. / Sakamoto, H. / Kigawa, T. / Takio, K. / Shimura, Y. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal. Authors: Inoue, M. / Muto, Y. / Sakamoto, H. / Kigawa, T. / Takio, K. / Shimura, Y. / Yokoyama, S. #1: ![]() Title: Crystal Structure at 1.92 A Resolution of the RNA-Binding Domain of the U1A Spliceosomal Protein Complexed with an RNA Hairpin Authors: Oubridge, C. / Ito, N. / Evans, P.R. / Teo, C.H. / Nagai, K. #2: ![]() Title: Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-Lethal Determined by Multidimensional Heteronuclear Magnetic Resonance Authors: Lee, A.L. / Kanaar, R. / Rio, D.C. / Wemmer, D.E. #3: ![]() Title: Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian Hnrnp A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy Authors: Garrett, D.S. / Lodi, P.J. / Shamoo, Y. / Williams, K.R. / Clore, G.M. / Gronenborn, A.M. #4: ![]() Title: 1H, 13C, and 15N NMR Assignments and Global Folding Pattern of the RNA-Binding Domain of the Human Hnrnp C Proteins Authors: Wittekind, M. / Gorlach, M. / Friedrichs, M. / Dreyfuss, G. / Mueller, L. #5: ![]() Title: Crystal Structure of the RNA-Binding Domain of the U1 Small Nuclear Ribonucleoprotein A Authors: Nagai, K. / Oubridge, C. / Jessen, T.H. / Li, J. / Evans, P.R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 42.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 30.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 245.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 245.4 KB | Display | |
Data in XML | ![]() | 4.7 KB | Display | |
Data in CIF | ![]() | 5.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 10061.507 Da / Num. of mol.: 1 / Fragment: RNA-BINDING DOMAIN 1 (RBD1), RESIDUES 122 - 209 / Mutation: F166Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Sample conditions | pH: 4.0 / Temperature: 298 K |
---|---|
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software |
| ||||||||||||
Refinement | Method: HYBRID DISTANCE GEOMETRY, SIMULATED ANNEALING METHOD Software ordinal: 1 Details: REFINEMENT WAS DONE USING THE HYBRID DISTANCE GEOMETRY/SIMULATED ANNEALING METHOD (NILGES, M., CLORE, G.M., & GRONENBORN, A.M. (1988) FEBS LETT 229, 317-324) AS CONTAINED IN X-PLOR PROGRAM ...Details: REFINEMENT WAS DONE USING THE HYBRID DISTANCE GEOMETRY/SIMULATED ANNEALING METHOD (NILGES, M., CLORE, G.M., & GRONENBORN, A.M. (1988) FEBS LETT 229, 317-324) AS CONTAINED IN X-PLOR PROGRAM VERSION 3.1 (BRUNGER, 1992). THE RMSD FOR THE BACKBONE COORDINATES OF THE 20 STRUCTURES ACCEPTED AFTER THE LAST ROUND OF REFINEMENT COMPARED TO THE AVERAGE COORDINATES WAS 0.86 (FOR RESIDUES INVOLVED IN SECONDARY STRUCTURE). | ||||||||||||
NMR ensemble | Conformer selection criteria: SMALLEST RESIDUAL ENERGY / Conformers calculated total number: 200 / Conformers submitted total number: 1 |