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2KUM

Solution structure of the human chemokine CCL27

Summary for 2KUM
Entry DOI10.2210/pdb2kum/pdb
NMR InformationBMRB: 16839
DescriptorC-C motif chemokine 27 (1 entity in total)
Functional Keywordsccl27, ctack, chemokine, cytokine, disulfide bond, polymorphism, signaling protein
Biological sourceHomo sapiens (human)
Cellular locationSecreted: Q9Y4X3
Total number of polymer chains1
Total formula weight10165.93
Authors
Kirkpatrick, J.P.,Jansma, A.,Hsu, A.,Handel, T.M.,Nietlispach, D. (deposition date: 2010-02-22, release date: 2010-03-02, Last modification date: 2024-10-30)
Primary citationJansma, A.L.,Kirkpatrick, J.P.,Hsu, A.R.,Handel, T.M.,Nietlispach, D.
NMR analysis of the structure, dynamics, and unique oligomerization properties of the chemokine CCL27.
J.Biol.Chem., 285:14424-14437, 2010
Cited by
PubMed Abstract: Chemokines have two essential interactions in vivo, with G protein-coupled receptors, which activate intracellular signaling pathways, and with glycosaminoglycans (GAGs), which are involved in cell surface localization and transport. Although it has been shown that chemokines bind and activate their respective G protein-coupled receptors as monomers, many chemokines oligomerize upon GAG binding, and the ability to oligomerize and bind GAGs is required for in vivo function. In this study, we investigated the structure, dynamics, and oligomerization behavior of cutaneous T-cell-attracting chemokine (CTACK, also known as CCL27) by NMR. (15)N relaxation and translational self-diffusion rates indicate that CCL27 oligomerizes, but in contrast to many other chemokines that form relatively discrete oligomers, CCL27 transitions between monomer, dimer, and tetramer species over a relatively narrow concentration range. A three-dimensional structure determination was pursued under conditions where CCL27 is primarily dimeric, revealing the standard motif for a chemokine monomer. Analysis of chemical shift perturbations of (1)H-(15)N HSQC spectra, relaxation-dispersion experiments, and filtered nuclear Overhauser effects suggest that CCL27 does not adopt a discrete CXC or CC dimer motif. Instead, CCL27 has uncommon oligomerization behavior, where several equilibria involving relatively low affinity interactions between different interfaces seem to be simultaneously at work. However, interaction with heparin avidly promotes oligomerization under conditions where CCL27 is monomeric by itself. We hypothesize that the plasticity in the oligomerization state may enable CCL27 to adopt different oligomeric structures, depending on the nature of the GAG binding partner, thereby providing a mechanism for increased diversity and specificity in GAG-binding and GAG-related functions.
PubMed: 20200157
DOI: 10.1074/jbc.M109.091108
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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