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1NR4

High resolution crystal structures of thymus and activation-regulated chemokine

Summary for 1NR4
Entry DOI10.2210/pdb1nr4/pdb
Related1NR2
DescriptorThymus and activation-regulated chemokine, SULFATE ION (3 entities in total)
Functional Keywordstarc, chemokine, cytokine, cc-chemokine, chemotaxis
Total number of polymer chains8
Total formula weight65346.71
Authors
Asojo, O.A.,Boulegue, C.,Hoover, D.M.,Lu, W.,Lubkowski, J. (deposition date: 2003-01-23, release date: 2003-08-05, Last modification date: 2024-10-16)
Primary citationAsojo, O.A.,Boulegue, C.,Hoover, D.M.,Lu, W.,Lubkowski, J.
Structures of thymus and activation-regulated chemokine (TARC).
Acta Crystallogr.,Sect.D, 59:1165-1173, 2003
Cited by
PubMed Abstract: Thymus and activation-regulated chemokine (TARC) is a CC chemokine that is mainly expressed in the thymus. TARC interacts primarily with the CCR4 receptor and to a lesser extent with the CCR8 receptor. The structures of TARC have been solved by molecular replacement in two space groups, triclinic (P1) and tetragonal (P4(1)), and refined to resolutions of 1.72 and 2.1 A, respectively, with R factors of 19.8% (R(free) = 24.1%) and 19.8% (R(free) = 27.7%), respectively. The search model originated from the crystal structure of another chemokine, RANTES, and proved to be only modestly similar to the refined structure of TARC. Whereas the tetragonal structure was easily solved using the program AMoRe, solution of the triclinic structure proved to be quite challenging and was obtained by combining the results from four different molecular-replacement programs (AMoRe, CNS, BEAST and EPMR), with subsequent extension of the gathered information. The tertiary structure of TARC is similar to that of other CC chemokines, with a three-stranded antiparallel beta-sheet flanked by a C-terminal helix. Both quaternary structures consist of dimers, which in the triclinic crystals pack further into tetramers. The TARC dimers are similar to those observed previously in the crystal structures of both MCP-1 and RANTES.
PubMed: 12832759
DOI: 10.1107/S0907444903009454
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.72 Å)
Structure validation

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