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- PDB-1sxl: RESONANCE ASSIGNMENTS AND SOLUTION STRUCTURE OF THE SECOND RNA-BI... -
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Basic information
Entry | Database: PDB / ID: 1sxl | ||||||
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Title | RESONANCE ASSIGNMENTS AND SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN OF SEX-LETHAL DETERMINED BY MULTIDIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE SPECTROSCOPY | ||||||
![]() | SEX-LETHAL PROTEIN PROTEIN | ||||||
![]() | RNA BINDING PROTEIN / RNA-BINDING PROTEIN | ||||||
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 | ||||||
![]() | Lee, A.L. / Kanaar, R. / Rio, D.C. / Wemmer, D.E. | ||||||
![]() | ![]() 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. #1: ![]() 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. #2: ![]() 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. / Goerlach, M. / Friedrichs, M. / Dreyfuss, G. / Mueller, L. #3: ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 508.7 KB | Display | ![]() |
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PDB format | ![]() | 420.3 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 342.6 KB | Display | ![]() |
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Full document | ![]() | 602.2 KB | Display | |
Data in XML | ![]() | 67.2 KB | Display | |
Data in CIF | ![]() | 90.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 10790.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 17 |