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http://purl.uniprot.org/citations/11601972http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11601972http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11601972http://www.w3.org/2000/01/rdf-schema#comment"Lymphotactin, the sole identified member of the C class of chemokines, specifically attracts T lymphocytes and natural killer cells. This 93-residue protein lacks 2 of the 4 conserved cysteine residues characteristic of the other 3 classes of chemokines and possesses an extended carboxyl terminus, which is required for chemotactic activity. We have determined the three-dimensional solution structure of recombinant human lymphotactin by NMR spectroscopy. Under the conditions used for the structure determination, lymphotactin was predominantly monomeric; however, pulsed field gradient NMR self-diffusion measurements and analytical ultracentrifugation revealed evidence of dimer formation. Sequence-specific chemical shift assignments were determined through analysis of two- and three-dimensional NMR spectra of (15)N- and (13)C/(15)N-enriched protein samples. Input for the torsion angle dynamics calculations used in determining the structure included 1258 unique NOE-derived distance constraints and 60 dihedral angle constraints obtained from chemical-shift-based searching of a protein conformational database. The ensemble of 20 structures chosen to represent the structure had backbone and heavy atom rms deviations of 0.46 +/- 0.11 and 1.02 +/-0.14 A, respectively. The results revealed that human lymphotactin adopts the conserved chemokine fold, which is characterized by a three-stranded antiparallel beta-sheet and a C-terminal alpha-helix. Two regions are dynamically disordered as evidenced by (1)H and (13)C chemical shifts and [(15)N]-(1)H NOEs: residues 1-9 of the amino terminus and residues 69-93 of the C-terminal extension. A functional role for the C-terminal extension, which is unique to lymphotactin, remains to be elucidated."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.org/dc/terms/identifier"doi:10.1021/bi011106p"xsd:string
http://purl.uniprot.org/citations/11601972http://purl.org/dc/terms/identifier"doi:10.1021/bi011106p"xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Markley J.L."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Markley J.L."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Volkman B.F."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"McCaslin D.R."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"McCaslin D.R."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Pauza C.D."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Pauza C.D."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Kitabwalla M."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Kitabwalla M."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Kuloglu E.S."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/author"Kuloglu E.S."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/pages"12486-12496"xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/pages"12486-12496"xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/title"Monomeric solution structure of the prototypical 'C' chemokine lymphotactin."xsd:string
http://purl.uniprot.org/citations/11601972http://purl.uniprot.org/core/title"Monomeric solution structure of the prototypical 'C' chemokine lymphotactin."xsd:string