Structural bioinformatics of the human spliceosomal proteome.

Nucleic Acids Research
Iga KornetaJanusz M Bujnicki

Abstract

In this work, we describe the results of a comprehensive structural bioinformatics analysis of the spliceosomal proteome. We used fold recognition analysis to complement prior data on the ordered domains of 252 human splicing proteins. Examples of newly identified domains include a PWI domain in the U5 snRNP protein 200K (hBrr2, residues 258-338), while examples of previously known domains with a newly determined fold include the DUF1115 domain of the U4/U6 di-snRNP protein 90K (hPrp3, residues 540-683). We also established a non-redundant set of experimental models of spliceosomal proteins, as well as constructed in silico models for regions without an experimental structure. The combined set of structural models is available for download. Altogether, over 90% of the ordered regions of the spliceosomal proteome can be represented structurally with a high degree of confidence. We analyzed the reduced spliceosomal proteome of the intron-poor organism Giardia lamblia, and as a result, we proposed a candidate set of ordered structural regions necessary for a functional spliceosome. The results of this work will aid experimental and structural analyses of the spliceosomal proteins and complexes, and can serve as a starting point fo...Continue Reading

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Nov 17, 2012·Nucleic Acids Research·Kaja MilanowskaJanusz M Bujnicki
Nov 3, 2012·Nucleic Acids Research·Ivan Cvitkovic, Melissa S Jurica
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Methods Mentioned

BETA
X-ray
NMR
protein folding

Software Mentioned

SpliProt3D
ROSETTA
MODELLER
CLANS
DALI
BLAST
PCONS
GeneSilico MetaServer gateway
BLASTP
UCSF Chimera

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