Clay Barreto Rios

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Three-dimensional structures of complexes of the SH2 domain of the v-src oncogene product with two phosphotyrosyl peptides have been determined by X-ray crystallography at resolutions of 1.5 and 2.0 A, respectively. A central antiparallel beta-sheet in the structure is flanked by two alpha-helices, with peptide binding mediated by the sheet, intervening(More)
A three-disulfide intermediate, des-[65-72] RNase A, lacking the disulfide bond between Cys65 and Cys72, is formed in one of the rate-determining steps of the oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A). An analog of this intermediate, [C65S, C72S] RNase A, has been characterized in terms of structure and thermodynamic(More)
The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2' forms a novel arginine-rich nucleic acid binding motif.
SH2 regions are protein motifs capable of binding target protein sequences that contain a phosphotyrosine. The solution structure of the abl SH2 product, a protein of 109 residues and 12.1 kd, has been determined by multidimensional nuclear magnetic resonance spectroscopy. It is a compact spherical domain with a pair of three-stranded antiparallel beta(More)
Triple-resonance experiments can be designed to provide useful information on spin-system topologies. In this paper we demonstrate optimized proton and carbon versions of PFG-CT-HACANH and PFG-CT-HACA(CO)NH 'straight-through' triple-resonance experiments that allow rapid and almost complete assignments of backbone H(alpha), 13C(alpha), 15N and H(N)(More)
Triple-resonance experiments facilitate the determination of sequence-specific resonance assignments of medium-sized 13C,15N-enriched proteins. Some triple-resonance experiments can also be used to obtain information about amino acid spin-system topologies by proper delay tuning. The constant-time PFG-CBCA(CO)NH experiment allows discrimination between five(More)
BACKGROUND More recently, the association of different risk factors has been described as the metabolic syndrome. Different definitions are being used for the same syndrome. Regardless of the name or classification, it has been well established that a cardiovascular cluster including overweight/obesity, increased blood pressure, and lipid and glucose(More)
Many triple-resonance experiments make use of one-bond heteronuclear scalar couplings toestablish connectivities among backbone and/or side-chain nuclei. In medium-sized(15-30 kDa) proteins, short transverse relaxation times of Calpha single-quantum stateslimit signal-to-noise (S/N) ratios. These relaxation properties can be improved usingheteronuclear(More)
The Src homology 2 (SH2) domain is a recognition motif thought to mediate the association of the cytoplasmic proteins involved in signal transduction by binding to phosphotyrosyl-containing sequences in proteins. Assignments of nearly all 1H and 15N resonances of the SH2 domain from the c-Abl protein-tyrosine kinase have been obtained from homonuclear and(More)
We have developed a useful strategy for identifying amino acid spin systems and side-chain carbon resonance assignments in small 15N-, 13C-enriched proteins. Multidimensional constant-time pulsed field gradient (PFG) HCC(CO)NH-TOCSY experiments provide side-chain resonance frequency information and establish connectivities between sequential amino acid spin(More)
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