2f9d

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(New page: 200px<br /> <applet load="2f9d" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f9d, resolution 2.50&Aring;" /> '''2.5 angstrom resolu...)
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<applet load="2f9d" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2f9d, resolution 2.50&Aring;" />
caption="2f9d, resolution 2.50&Aring;" />
'''2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155'''<br />
'''2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155'''<br />
==Overview==
==Overview==
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The precise excision of introns from precursor mRNAs (pre-mRNAs) in, eukaryotes is accomplished by the spliceosome, a complex assembly, containing five small nuclear ribonucleoprotein (snRNP) particles. Human, p14, a component of the spliceosomal U2 and U11/U12 snRNPs, has been shown, to associate directly with the pre-mRNA branch adenosine early in, spliceosome assembly and within the fully assembled spliceosome. Here we, report the 2.5-A crystal structure of a complex containing p14 and a, peptide derived from the p14-associated U2 snRNP component SF3b155. p14, contains an RNA recognition motif (RRM), the surface of which is largely, occluded by a C-terminal alpha-helix and a portion of the SF3b155 peptide., An analysis of RNA.protein crosslinking to wild-type and mutant p14 shows, that the branch adenosine directly interacts with a conserved aromatic, within a pocket on the surface of the complex. This result, combined with, a comparison of the structure with known RRMs and pseudoRRMs as well as, model-building by using the electron cryomicroscopy structure of a, spliceosomal U11/U12 di-snRNP, suggests that p14.SF3b155 presents a, noncanonical surface for RNA recognition at the heart of the mammalian, spliceosome.
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The precise excision of introns from precursor mRNAs (pre-mRNAs) in eukaryotes is accomplished by the spliceosome, a complex assembly containing five small nuclear ribonucleoprotein (snRNP) particles. Human p14, a component of the spliceosomal U2 and U11/U12 snRNPs, has been shown to associate directly with the pre-mRNA branch adenosine early in spliceosome assembly and within the fully assembled spliceosome. Here we report the 2.5-A crystal structure of a complex containing p14 and a peptide derived from the p14-associated U2 snRNP component SF3b155. p14 contains an RNA recognition motif (RRM), the surface of which is largely occluded by a C-terminal alpha-helix and a portion of the SF3b155 peptide. An analysis of RNA.protein crosslinking to wild-type and mutant p14 shows that the branch adenosine directly interacts with a conserved aromatic within a pocket on the surface of the complex. This result, combined with a comparison of the structure with known RRMs and pseudoRRMs as well as model-building by using the electron cryomicroscopy structure of a spliceosomal U11/U12 di-snRNP, suggests that p14.SF3b155 presents a noncanonical surface for RNA recognition at the heart of the mammalian spliceosome.
==About this Structure==
==About this Structure==
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2F9D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F9D OCA].
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2F9D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9D OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Edwards, R.A.]]
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[[Category: Edwards, R A.]]
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[[Category: Glover, J.N.M.]]
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[[Category: Glover, J N.M.]]
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[[Category: Macmillan, A.M.]]
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[[Category: Macmillan, A M.]]
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[[Category: Ritchie, D.B.]]
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[[Category: Ritchie, D B.]]
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[[Category: Schellenberg, M.J.]]
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[[Category: Schellenberg, M J.]]
[[Category: p14 sf3bp14 sf3b155 sap155 rrm]]
[[Category: p14 sf3bp14 sf3b155 sap155 rrm]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:01:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:04 2008''

Revision as of 15:19, 21 February 2008


2f9d, resolution 2.50Å

Drag the structure with the mouse to rotate

2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155

Overview

The precise excision of introns from precursor mRNAs (pre-mRNAs) in eukaryotes is accomplished by the spliceosome, a complex assembly containing five small nuclear ribonucleoprotein (snRNP) particles. Human p14, a component of the spliceosomal U2 and U11/U12 snRNPs, has been shown to associate directly with the pre-mRNA branch adenosine early in spliceosome assembly and within the fully assembled spliceosome. Here we report the 2.5-A crystal structure of a complex containing p14 and a peptide derived from the p14-associated U2 snRNP component SF3b155. p14 contains an RNA recognition motif (RRM), the surface of which is largely occluded by a C-terminal alpha-helix and a portion of the SF3b155 peptide. An analysis of RNA.protein crosslinking to wild-type and mutant p14 shows that the branch adenosine directly interacts with a conserved aromatic within a pocket on the surface of the complex. This result, combined with a comparison of the structure with known RRMs and pseudoRRMs as well as model-building by using the electron cryomicroscopy structure of a spliceosomal U11/U12 di-snRNP, suggests that p14.SF3b155 presents a noncanonical surface for RNA recognition at the heart of the mammalian spliceosome.

About this Structure

2F9D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a core spliceosomal protein interface., Schellenberg MJ, Edwards RA, Ritchie DB, Kent OA, Golas MM, Stark H, Luhrmann R, Glover JN, MacMillan AM, Proc Natl Acad Sci U S A. 2006 Jan 31;103(5):1266-71. Epub 2006 Jan 23. PMID:16432215

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