1j9o
From Proteopedia
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'''SOLUTION STRUCTURE OF HUMAN LYMPHOTACTIN''' | '''SOLUTION STRUCTURE OF HUMAN LYMPHOTACTIN''' | ||
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[[Category: Pauza, C D.]] | [[Category: Pauza, C D.]] | ||
[[Category: Volkman, B F.]] | [[Category: Volkman, B F.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:57:20 2008'' | |
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Revision as of 17:57, 2 May 2008
SOLUTION STRUCTURE OF HUMAN LYMPHOTACTIN
Overview
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.
About this Structure
1J9O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Monomeric solution structure of the prototypical 'C' chemokine lymphotactin., Kuloglu ES, McCaslin DR, Kitabwalla M, Pauza CD, Markley JL, Volkman BF, Biochemistry. 2001 Oct 23;40(42):12486-96. PMID:11601972 Page seeded by OCA on Fri May 2 20:57:20 2008
