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See also Receptor
TNF receptor superfamily
The extracellular domain of TNFR contains 2 to 6 cysteine-rich domains (CRD). The . The CRDs are involved in binding of TNF[1]. . Water molecules are shown as red spheres.
TRAIL-R2 is called DR5. (1d0g).
Colony-stimulating factor receptor
The via the conserved kinase DFG motif (colored in salmon) and its gatekeeper threonine residue (colored in magenta)[2].
The structure of the complex between M-CSF and its receptor shows that a . There are [3]. .
Type I cytokine receptors
The of the blood marrow is part of the hematipoietic cytokine family. This receptor has a single transmembrane domain, that forms a homodimer complex until it is activated by the binding of EPO. This receptor is 484 amino acids long and weigh 52.6 kDa. Once the homodimer is formed after the binding, autophosphorlation of the Jak2 kinases, which activates other cellular processes. This transmembrane receptor has two extracellular domains. This receptor has two disulfide bonds that are formed from 4 cystine residues, . The intracellular domain of this receptor does not possess any enzymatic activity like other receptors. When EPO comes in contact with the extracellular domains form a ligand bond. The extracellular sinding site 1 and Binding site 2 are composed of . When EPO binds, all loops on D1 and D2 of binding site one form a bind with EPO. However loop 4 of D1 on binding site 2 does not participate in the binding of EPO [4]. After the biniding of EPO, 8 tyrosine residues are phosphoralated which activates the . This kinase helps regulate the transcription of different genes and expression of other proteins.
(PDB code 1cn4).[5]
(PDB code 3mzg). The interaction between PRLR and prolactin is strongly pH-dependent and is critically dependent on [6]. Water molecules are shown as red spheres. .
Type II cytokine receptors
Interferon receptors
Interleukin receptors
Interleukin-20 receptor:
