Related ArticlesStructural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy.
Biochemistry. 2000 Nov 7;39(44):13602-13
Authors: Sayers EW, Gerstner RB, Draper DE, Torchia DA
Protein S4, a component of the 30S subunit of the prokaryotic ribosome, is one of the first proteins to interact with rRNA in the process of ribosome assembly and is known to be involved in the regulation of this process. While the structure of the C-terminal 158 residues of Bacillus stearothermophilus S4 has been solved by both X-ray crystallography and NMR, that of the N-terminal 41 residues is unknown. Evidence suggests that the N-terminus is necessary both for the assembly of functional ribosomes and for full binding to 16S RNA, and so we present NMR data collected on the full-length protein (200 aa). Our data indicate that the addition of the N-terminal residues does not significantly change the structure of the C-terminal 158 residues. The data further indicate that the N-terminus is highly flexible in solution, without discernible secondary structure. Nevertheless, structure calculations based on nuclear Overhauser effect spectroscopic data combined with (15)N relaxation data revealed that two short segments in the N-terminus, S(12)RRL(15) and P(30)YPP(33), adopt transiently ordered states in solution. The major conformation of S(12)RRL(15) appears to orient the arginine side chains outward toward the solvent in a parallel fashion, while that of P(30)YPP(33) forms a nascent turn of a polyproline II helix. These segments contain residues that are highly conserved across many prokaryotic species, and thus they are reasonable candidates respectively for sites of interaction with RNA and other ribosomal proteins within the intact ribosome.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
[NMR paper] Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis,
Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches.
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Structure. 2004 Apr;12(4):633-44
Authors: Dominguez C, Bonvin AM, Winkler GS, van Schaik FM, Timmers HT, Boelens R
The protein CNOT4 possesses an N-terminal RING finger domain that acts as an E3 ubiquitin ligase and specifically interacts with UbcH5B, a ubiquitin-conjugating enzyme. The structure of the CNOT4...
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[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
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[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
...
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[NMR paper] Determination of the structure of the N-terminal splice region of the cyclic AMP-spec
Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructs.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructs.
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[NMR paper] Structural and dynamic characterization of the phosphotyrosine binding region of a Sr
Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
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Biochemistry. 1995 Sep 12;34(36):11353-62
Authors: Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD
Arginine side chains are often...
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[NMR paper] The carboxyl-terminal region of human interferon gamma is important for biological ac
The carboxyl-terminal region of human interferon gamma is important for biological activity: mutagenic and NMR analysis.
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Protein Eng. 1991 Feb;4(3):335-41
Authors: Lundell D, Lunn C, Dalgarno D, Fossetta J, Greenberg R, Reim R, Grace M, Narula S
Deletion of nine amino acids from the carboxyl terminus of human IFN gamma (residues 138--146; LFRGRRASQ) resulted in a 7-fold increase in specific antiviral...
Structural preordering in the N-terminal region of ribosomal protein S4 revealed by h
Linear Mode
