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PDBsum entry 1sxl

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RNA binding protein PDB id
1sxl
Contents
Protein chain
97 a.a.

References listed in PDB file
Key reference
Title Resonance assignments and solution structure of the second RNA-Binding domain of sex-Lethal determined by multidimensional heteronuclear magnetic resonance.
Authors A.L.Lee, R.Kanaar, D.C.Rio, D.E.Wemmer.
Ref. Biochemistry, 1994, 33, 13775-13786. [DOI no: 10.1021/bi00250a031]
PubMed id 7524663
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 96%.
Abstract
The RNA-binding protein Sex-lethal (Sxl) is a critical regulator of sexual differentiation and dosage compensation in Drosophila. This regulatory activity is a consequence of the ability of Sxl to bind uridine-rich RNA tracts involved in pre-mRNA splicing. Sxl contains two RNP consensus-type RNA-binding domains (RBDs). A structural study of a portion of Sxl (amino acids 199-294) containing the second RNA-binding domain (RBD-2) using multidimensional heteronuclear NMR is presented here. Nearly complete 1H, 13C, and 15N resonance assignments have been obtained from 15N- and 13C/15N-uniformly labeled protein. These assignments were used to analyze 3D 15N-separated NOESY and 13C/13C-separated 4D NOESY spectra which produced 494 total and 169 long-range NOE-derived distance restraints. Along with 41 backbone dihedral restraints, these distance restraints were employed to generate an intermediate-resolution family of calculated structures, which exhibits the beta alpha beta-beta alpha beta tertiary fold found in other RBD-containing proteins. The RMSD to the average structure for the backbone atoms of residues 11-93 is 1.55 +/- 0.30 A, while the RMSD for backbone atoms involved in secondary structure is 0.76 +/- 0.14 A. A capping box [Harper, E.T., & Rose, G.D. (1993) Biochemistry 32, 7605-7609] was identified at the N-terminus of the first helix and has been characterized by short- and medium-range NOEs. Finally, significant structural similarities and differences between Sxl RBD-2 and other RBD-containing proteins are discussed.
Secondary reference #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 D.S.Garrett, P.J.Lodi, Y.Shamoo, K.R.Williams, G.M.Clore, A.M.Gronenborn.
Ref. Biochemistry, 1994, 33, 2852-2858. [DOI no: 10.1021/bi00176a015]
PubMed id 8130198
Full text Abstract
Secondary reference #2
Title 1h, 13c, And 15n nmr assignments and global folding pattern of the RNA-Binding domain of the human hnrnp c proteins.
Authors M.Wittekind, M.Görlach, M.Friedrichs, G.Dreyfuss, L.Mueller.
Ref. Biochemistry, 1992, 31, 6254-6265. [DOI no: 10.1021/bi00142a013]
PubMed id 1385725
Full text Abstract
Secondary reference #3
Title Crystal structure of the RNA-Binding domain of the u1 small nuclear ribonucleoprotein a.
Authors K.Nagai, C.Oubridge, T.H.Jessen, J.Li, P.R.Evans.
Ref. Nature, 1990, 348, 515-520.
PubMed id 2147232
Abstract
PROCHECK
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