1fjc: Difference between revisions
New page: left|200px<br /><applet load="1fjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjc" /> '''SOLUTION STRUCTURE OF NUCLEOLIN RBD2'''<br /... |
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'''SOLUTION STRUCTURE OF NUCLEOLIN RBD2'''<br /> | '''SOLUTION STRUCTURE OF NUCLEOLIN RBD2'''<br /> | ||
==Overview== | ==Overview== | ||
Nucleolin is an abundant 70 kDa nucleolar protein involved in many aspects | 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'. | ||
==About this Structure== | ==About this Structure== | ||
1FJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full crystallographic information is available from [http:// | 1FJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mesocricetus auratus]] | [[Category: Mesocricetus auratus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Allain, F | [[Category: Allain, F H.T.]] | ||
[[Category: Bouvet, P.]] | [[Category: Bouvet, P.]] | ||
[[Category: Feigon, J.]] | [[Category: Feigon, J.]] | ||
[[Category: Gilbert, D | [[Category: Gilbert, D E.]] | ||
[[Category: nucleolus]] | [[Category: nucleolus]] | ||
[[Category: rbd]] | [[Category: rbd]] | ||
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[[Category: rrm]] | [[Category: rrm]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:16 2008'' | ||
Revision as of 13:39, 21 February 2008
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SOLUTION STRUCTURE OF NUCLEOLIN RBD2
OverviewOverview
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'.
About this StructureAbout this Structure
1FJC is a Single protein structure of sequence from Mesocricetus auratus. Full crystallographic information is available from OCA.
ReferenceReference
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
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