Related ArticlesSolution 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
Authors: Allain FH, Gilbert DE, Bouvet P, Feigon J
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, dynamics and thermodynamics of the three SH3 domains of CD2AP
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Abstract CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability...
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[NMR paper] NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Related Articles NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Biochemistry. 2004 Nov 30;43(47):14940-7
Authors: Biverståhl H, Andersson A, Gräslund A, Mäler L
The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy...
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[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
...
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[NMR paper] Yeast heat shock transcription factor N-terminal activation domains are unstructured
Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
Protein Sci. 1996 Feb;5(2):262-9...
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Solution structure of the RBD1,2 domains from human nucleolin
Solution structure of the RBD1,2 domains from human nucleolin
Content Type Journal Article
DOI 10.1007/s10858-010-9412-1
Authors
Sengodagounder Arumugam, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
M. Clarke Miller, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
James Maliekal, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR stu
Linear Mode
