CCR1

HM145, LD78 receptor, Macrophage inflammatory protein 1-alpha receptor, MIP-1alpha-R

CCR1
C-C chemokine receptor type 1
Andere Namen

HM145, LD78 receptor, Macrophage inflammatory protein 1-alpha receptor, MIP-1alpha-R

Vorhandene Strukturdaten: PDB 1Y5D

Eigenschaften des menschlichen Proteins
Masse/Länge Primärstruktur 355 Aminosäuren, 41.173 Da
Bezeichner
Externe IDs
Vorkommen
Homologie-Familie Hovergen
Orthologe (Mensch)
Entrez 1230
Ensembl ENSG00000163823
UniProt P32246
Refseq (mRNA) NM_001295.2
Refseq (Protein) NP_001286.1
PubMed-Suche 1230

Genexpressionsmuster des CCR1-Gens.

C-C chemokine receptor type 1 (CCR1) ist ein Oberflächenprotein aus der Gruppe der Chemokinrezeptoren.

Eigenschaften

CCR1 ist ein G-Protein-gekoppelter Rezeptor[1] und wird von verschiedenen hämatopoetischen Zellen gebildet. Er bindet Chemokine vom C-C-Typ wie MIP-1-alpha (CCL3), MIP-1-delta, RANTES (CCL5)[2][3] und MCP-3 (CCL7). Mit geringerer Affinität wird MIP-1-beta und MCP-1 gebunden. Nach Bindung steigt die zelluläre Konzentration des second messenger Ca2+. CCR1 ist glykosyliert und phosphoryliert.

CCR1 wird zur Behandlung von Autoimmunerkrankungen und Infektionskrankheiten untersucht.[4]

Einzelnachweise

  1. ↑ A. Karash, M. R. Mazzoni, A. Gilchrist: Pharmacological intervention at CCR1 and CCR5 as an approach for cancer: help or hindrance. In: Current topics in medicinal chemistry. Band 14, Nummer 13, 2014, S. 1553–1573, PMID 25159162.
  2. ↑ Struyf S, Menten P, Lenaerts JP, Put W, D’Haese A, De Clercq E, Schols D, Proost P, Van Damme J: Diverging binding capacities of natural LD78beta isoforms of macrophage inflammatory protein-1alpha to the CC chemokine receptors 1, 3 and 5 affect their anti-HIV-1 activity and chemotactic potencies for neutrophils and eosinophils. In: European Journal of Immunology. 31. Jahrgang, Nr. 7, Juli 2001, S. 2170–8, doi:10.1002/1521-4141(200107)31:7<2170::AID-IMMU2170>3.0.CO;2-D, PMID 11449371 (englisch).
  3. ↑ Proudfoot AE, Fritchley S, Borlat F, Shaw JP, Vilbois F, Zwahlen C, Trkola A, Marchant D, Clapham PR, Wells TN: The BBXB motif of RANTES is the principal site for heparin binding and controls receptor selectivity. In: The Journal of Biological Chemistry. 276. Jahrgang, Nr. 14, April 2001, S. 10620–6, doi:10.1074/jbc.M010867200, PMID 11116158 (englisch).
  4. ↑ H. W. Zimmermann, V. Sterzer, H. Sahin: CCR1 and CCR2 antagonists. In: Current topics in medicinal chemistry. Band 14, Nummer 13, 2014, S. 1539–1552, PMID 25159163.

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