1e7k: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (19 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment== | |||
<StructureSection load='1e7k' size='340' side='right'caption='[[1e7k]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
| | == Structural highlights == | ||
| | <table><tr><td colspan='2'>[[1e7k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E7K FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7k OCA], [https://pdbe.org/1e7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e7k RCSB], [https://www.ebi.ac.uk/pdbsum/1e7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7k ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NH2L1_HUMAN NH2L1_HUMAN] Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.<ref>PMID:10545122</ref> <ref>PMID:17412961</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e7/1e7k_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e7k ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have determined the crystal structure of a spliceosomal RNP complex comprising the 15.5kD protein of the human U4/U6.U5 tri-snRNP and the 5' stem-loop of U4 snRNA. The protein interacts almost exclusively with a purine-rich (5+2) internal loop within the 5' stem-loop, giving an unusual RNA fold characterized by two tandem sheared G-A base pairs, a high degree of purine stacking, and the accommodation of a single RNA base, rotated out of the RNA chain, in a pocket of the protein. Apart from yielding the structure of an important entity in the pre-mRNA splicing apparatus, this work also implies a model for the complex of the 15.5kD protein with box C/D snoRNAs. It additionally suggests a general recognition principle in a novel family of RNA binding proteins. | |||
Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment.,Vidovic I, Nottrott S, Hartmuth K, Luhrmann R, Ficner R Mol Cell. 2000 Dec;6(6):1331-42. PMID:11163207<ref>PMID:11163207</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1e7k" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Kink-turn motif|Kink-turn motif]] | |||
*[[User:Wayne Decatur/kink-turn motif|User:Wayne Decatur/kink-turn motif]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
== | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ficner | [[Category: Ficner R]] | ||
[[Category: Harthmuth | [[Category: Harthmuth K]] | ||
[[Category: Luhrmann | [[Category: Luhrmann R]] | ||
[[Category: Nottrott | [[Category: Nottrott S]] | ||
[[Category: Vidovic | [[Category: Vidovic I]] | ||
Latest revision as of 11:47, 9 May 2024
Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragmentCrystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment
Structural highlights
FunctionNH2L1_HUMAN Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the crystal structure of a spliceosomal RNP complex comprising the 15.5kD protein of the human U4/U6.U5 tri-snRNP and the 5' stem-loop of U4 snRNA. The protein interacts almost exclusively with a purine-rich (5+2) internal loop within the 5' stem-loop, giving an unusual RNA fold characterized by two tandem sheared G-A base pairs, a high degree of purine stacking, and the accommodation of a single RNA base, rotated out of the RNA chain, in a pocket of the protein. Apart from yielding the structure of an important entity in the pre-mRNA splicing apparatus, this work also implies a model for the complex of the 15.5kD protein with box C/D snoRNAs. It additionally suggests a general recognition principle in a novel family of RNA binding proteins. Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment.,Vidovic I, Nottrott S, Hartmuth K, Luhrmann R, Ficner R Mol Cell. 2000 Dec;6(6):1331-42. PMID:11163207[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||