Solution Structure of CCL19 and Identification of Overlapping CCR7 and PSGL-1 Binding Sites
| Autor: | Harley Pyles, Gary R. Chaffee, Scott J. Schoeller, Boris Touzeau, Miranda L. Gillitzer, Asha A. Bailey, Christopher T. Veldkamp, Emily R. Lackner, Larry G. Williams, Eva Kiermaier, Yaya Bah, Frank A. DiSilvio, Amanda M. Richard, Andrew J. Phillips, Paeton L. Wantuch, David R. Graupner, Michael L. Olson, David R. Lippner, Casey J. Mueller, Tysha Medeiros, Michael Sixt, Skylar J. Gabel-Eissens, Danielle M. Zgoba, Francis C. Peterson, Vincent D. LaRosa, Michael W. Famiglietti, Samantha J. Engebretson |
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| Rok vydání: | 2015 |
| Předmět: |
CCR1
Models Molecular Chemokine Receptors CCR7 Binding Sites Membrane Glycoproteins biology integumentary system Protein Conformation CCL19 C-C chemokine receptor type 7 chemical and pharmacologic phenomena Biochemistry Molecular biology Article Cell biology Chemokine receptor biology.protein Chemokine CCL19 Humans Binding site CXCL16 CCL21 |
| Zdroj: | Biochemistry. 54(27) |
| ISSN: | 1520-4995 |
| Popis: | CCL19 and CCL21 are chemokines involved in the trafficking of immune cells, particularly within the lymphatic system, through activation of CCR7. Concurrent expression of PSGL-1 and CCR7 in naive T-cells enhances recruitment of these cells to secondary lymphoid organs by CCL19 and CCL21. Here the solution structure of CCL19 is reported. It contains a canonical chemokine domain. Chemical shift mapping shows the N-termini of PSGL-1 and CCR7 have overlapping binding sites for CCL19 and binding is competitive. Implications for the mechanism of PSGL-1’s enhancement of resting T-cell recruitment are discussed. |
| Databáze: | OpenAIRE |
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