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| | ==SOLUTION STRUCTURE OF NUCLEOLIN RBD2== | | ==SOLUTION STRUCTURE OF NUCLEOLIN RBD2== |
| - | <StructureSection load='1fjc' size='340' side='right' caption='[[1fjc]], [[NMR_Ensembles_of_Models | 33 NMR models]]' scene=''> | + | <StructureSection load='1fjc' size='340' side='right'caption='[[1fjc]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1fjc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Golden_hamster Golden hamster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FJC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1fjc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fj7|1fj7]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjc OCA], [http://pdbe.org/1fjc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fjc RCSB], [http://www.ebi.ac.uk/pdbsum/1fjc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjc ProSAT]</span></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=1fjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjc OCA], [https://pdbe.org/1fjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fjc RCSB], [https://www.ebi.ac.uk/pdbsum/1fjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NUCL_MESAU NUCL_MESAU]] Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).<ref>PMID:3409881</ref> | + | [https://www.uniprot.org/uniprot/NUCL_MESAU NUCL_MESAU] Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).<ref>PMID:3409881</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1fjc" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1fjc" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Nucleolin|Nucleolin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Golden hamster]] | + | [[Category: Large Structures]] |
| - | [[Category: Allain, F H.T]] | + | [[Category: Mesocricetus auratus]] |
| - | [[Category: Bouvet, P]] | + | [[Category: Allain FH-T]] |
| - | [[Category: Feigon, J]] | + | [[Category: Bouvet P]] |
| - | [[Category: Gilbert, D E]] | + | [[Category: Feigon J]] |
| - | [[Category: Nucleolus]]
| + | [[Category: Gilbert DE]] |
| - | [[Category: Rbd]]
| + | |
| - | [[Category: Rna binding domain]]
| + | |
| - | [[Category: Rnp]]
| + | |
| - | [[Category: Rrm]]
| + | |
| - | [[Category: Structural protein]]
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| Structural highlights
Function
NUCL_MESAU Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).[1]
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 PubMed
Nucleolin is an abundant 70 kDa nucleolar protein involved in many aspects of ribosomal RNA biogenesis. The central region of nucleolin contains four tandem consensus RNA-binding domains (RBD). The two most N-terminal domains (RBD12) bind with nanomolar affinity to an RNA stem-loop containing the consensus sequence UCCCGA in the loop. We have determined the solution structure of nucleolin RBD12 in its free form and have studied its interaction with a 22 nt RNA stem-loop using multidimensional NMR spectroscopy. The two RBDs adopt the expected beta alpha beta beta alpha beta fold, but the position of the beta 2 strand in both domains differs from what was predicted from sequence alignments. RBD1 and RBD2 are significantly different from each others and this is likely important in their sequence specific recognition of the RNA. RBD1 has a longer alpha-helix 1 and a shorter beta 2-beta 3 loop than RBD2, and differs from most other RBDs in these respects. The two RBDs are separated by a 12 amino acid flexible linker and do not interact with one another in the free protein. This linker becomes ordered when RBD12 binds to the RNA. Analysis of the observed NOEs between the protein and the RNA indicates that both RBDs interact with the RNA loop via their beta-sheet. Each domain binds residues on one side of the loop; specifically, RBD2 contacts the 5' side and RBD1 contacts the 3'.
Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.,Allain FH, Gilbert DE, Bouvet P, Feigon J J Mol Biol. 2000 Oct 20;303(2):227-41. PMID:11023788[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Erard MS, Belenguer P, Caizergues-Ferrer M, Pantaloni A, Amalric F. A major nucleolar protein, nucleolin, induces chromatin decondensation by binding to histone H1. Eur J Biochem. 1988 Aug 15;175(3):525-30. PMID:3409881
- ↑ Allain FH, Gilbert DE, Bouvet P, Feigon J. Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target. J Mol Biol. 2000 Oct 20;303(2):227-41. PMID:11023788 doi:10.1006/jmbi.2000.4118
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