PDBsum entry: 1j8i

Cytokine

PDB id: 1j8i

Contents

Protein chain

93 a.a. *

* Residue conservation analysis

PDB id:

1j8i

Name:

Cytokine

Title:

Solution structure of human lymphotactin

Structure:

Lymphotactin. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

E.S.Kuloglu,D.R.Mccaslin,J.L.Markley,C.D.Pauza,B.F.Volkman

Key ref:

E.S.Kuloglu et al. (2001). Monomeric solution structure of the prototypical 'C' chemokine lymphotactin. Biochemistry, 40, 12486-12496. PubMed id: 11601972 DOI: 10.1021/bi011106p

Date:

21-May-01 Release date: 24-Oct-01

Protein chain

P47992  (XCL1_HUMAN) -  Lymphotactin

Seq: 114 a.a.

Struc: 93 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (2 terms)
• Biological process: immune response (5 terms)
• Biochemical function: cytokine activity (2 terms)

DOI no: 10.1021/bi011106p

Biochemistry 40:12486-12496 (2001)

PubMed id: 11601972

Monomeric solution structure of the prototypical 'C' chemokine lymphotactin.

E.S.Kuloglu, D.R.McCaslin, M.Kitabwalla, C.D.Pauza, J.L.Markley, B.F.Volkman.

ABSTRACT

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.