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Sandbox Reserved 939
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The structure of the C-terminal RNA recognition motif and an associated N-terminal extension (residues 380–517) of human U11/U12-65K has been determined by X-ray crystallography at 2.5 Å resolution<ref>PMID:19447915</ref> (<scene name='57/579709/3egn/5'>default view</scene>, coloring by secondary structure). The protein was crystallized in complex with an RNA oligonucleotide containing the loop and part of the stem of U12 snRNA stem-loop III; however, the oligonucleotide was not visible in the electron density. Residues 387-506 of the protein could be traced from the electron density map. | The structure of the C-terminal RNA recognition motif and an associated N-terminal extension (residues 380–517) of human U11/U12-65K has been determined by X-ray crystallography at 2.5 Å resolution<ref>PMID:19447915</ref> (<scene name='57/579709/3egn/5'>default view</scene>, coloring by secondary structure). The protein was crystallized in complex with an RNA oligonucleotide containing the loop and part of the stem of U12 snRNA stem-loop III; however, the oligonucleotide was not visible in the electron density. Residues 387-506 of the protein could be traced from the electron density map. | ||
| - | Residues 417–501 adopt a typical RRM fold, with an antiparallel four-stranded β-sheet packed against two α-helices. In addition to these canonical elements, the 65K C-terminal RRM contains a short helix between the α1 helix and the β2 strand and a β-hairpin in the loop connecting β2 and α2. Interestingly, as shown by electrophoretic mobility shift assays (EMSA), the core RRM fold of U11/U12-65K alone fails to bind to U12 snRNA. The core fold is stabilized by an N-terminal expansion comprising residues 380–417, which are required for RNA binding. <scene name='57/579709/Expansion/1'>The N-terminal expansion</scene> (shown in cyan) folds into two α-helices, a 3<sub>10</sub>-helix and a long loop that connects the expansion to the β1 strand. | + | Residues 417–501 adopt a typical RRM fold, with an antiparallel four-stranded β-sheet packed against two α-helices. In addition to these canonical elements, the 65K C-terminal RRM contains <scene name='57/579709/Shorthelix/1'>a short helix</scene> between the α1 helix and the β2 strand and a β-hairpin in the loop connecting β2 and α2. Interestingly, as shown by electrophoretic mobility shift assays (EMSA), the core RRM fold of U11/U12-65K alone fails to bind to U12 snRNA. The core fold is stabilized by an N-terminal expansion comprising residues 380–417, which are required for RNA binding. <scene name='57/579709/Expansion/1'>The N-terminal expansion</scene> (shown in cyan) folds into two α-helices, a 3<sub>10</sub>-helix and a long loop that connects the expansion to the β1 strand. |
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 14:54, 18 May 2014
| This Sandbox is Reserved from 01/04/2014, through 30/06/2014 for use in the course "510042. Protein structure, function and folding" taught by Prof Adrian Goldman, Tommi Kajander, Taru Meri, Konstantin Kogan and Juho Kellosalo at the University of Helsinki. This reservation includes Sandbox Reserved 923 through Sandbox Reserved 947. |
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