Related ArticlesRNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2495-9
Authors: Hoffman DW, Query CC, Golden BL, White SW, Keene JD
An RNA recognition motif (RRM) of approximately 80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human U1 small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel beta-strands and two alpha-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent beta-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.
4,4'-Dithiobis-dipicolinic Acid: A Small and Convenient Lanthanide Binding Tag for Protein NMR Spectroscopy.
4,4'-Dithiobis-dipicolinic Acid: A Small and Convenient Lanthanide Binding Tag for Protein NMR Spectroscopy.
4,4'-Dithiobis-dipicolinic Acid: A Small and Convenient Lanthanide Binding Tag for Protein NMR Spectroscopy.
Chemistry. 2011 May 3;
Authors: Jia X, Maleckis A, Huber T, Otting G
Pseudocontact shifts (PCS) from paramagnetic lanthanide ions present powerful long-range structure restraints for studies of proteins by nuclear magnetic resonance spectroscopy. To elicit PCSs, the lanthanide must be attached site-specifically to the target protein....
[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Related Articles NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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[NMR paper] The NMR structure of the sensory domain of the membranous two-component fumarate sens
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli.
J Biol Chem. 2003 Oct 3;278(40):39185-8
Authors: Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, Peti W, Zweckstetter M, Unden G, Griesinger C
The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined...
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[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...
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[NMR paper] NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear or
NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region...
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[NMR paper] The mobile loop region of the NAD(H) binding component (dI) of proton-translocating n
The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
Biochim Biophys Acta. 1999...
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[NMR paper] Structural changes in the recombinant, NADP(H)-binding component of proton translocat
Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy.
FEBS Lett. 1999 Mar 5;446(1):127-32
Authors: Quirk PG, Jeeves M, Cotton NP, Smith JK, Jackson BJ
We have analysed 1H, 15N-HSQC spectra of the...