New fibroblast growth factor receptor as defined in FGFR5 (FGFR) is identified by the EST database lymph node stromal cell cDNA library of mouse. And has an identity of about 32% of the extracellular domain of FGFR1-4 in EST. Library screening with this EST was identified alternative transcripts of two functions identified as gamma FGFR5 and FGFR5 Vector We. FGFR5 array whereas are included only two are FGFR5β, the main difference between the transfer of these is that the extracellular Ig domain contains three. It is that unique features of FGFR5, the intracellular tyrosine kinase domain that does not contain it. The predicted structure modeling of the extracellular domain of FGFR5 range, he suggests that it was a member of a subset of the I set of Ig superfamily of FGFR dove consistency known. Northern analysis of mouse and human showed that FGFR5 mRNA is detected in a wide range of tissues, including kidney, brain, and lung. The genome, we identified four introns, but there is no transcript of a completely different, including the tyrosine kinase domain. The extracellular region of γ5 and FGFR5β, was cloned Fc fragment of human IgG in (1) frame to produce a non-recombinant membrane protein. Instead of the FGF-2 ligand, R5 and recombinant FGFR5 Vector Fc in the Fc showed specific binding to EGF or FGF-7,. However, biological data indicates that FGF-2 binding to these proteins at lower affinity FGFR2C of the receptor analogs. The above data indicate that this receptor should be considered as the first member of the family of FGFR.

New fibroblast growth factor receptor as defined in FGFR5 (FGFR) is identified by the EST database lymph node stromal cell cDNA library of mouse. And has an identity of about 32% of the extracellular domain of FGFR1-4 in EST. Library screening with this EST was identified alternative transcripts of two functions identified as FGFR5γ and FGFR5β we. The main difference between these transcripts whereas that contain only one FGFR5γ2, its FGFR5β, extracellular Ig domain contains three. It is that unique features of FGFR5, the intracellular tyrosine kinase domain that does not contain it. The predicted structure modeling of the extracellular domain of FGFR5γ, he suggests that it was a member of a subset of the I set of Ig superfamily of FGFR dove consistency known. Northern analysis of mouse and human showed that FGFR5 mRNA is detected in a wide range of tissues, including kidney, brain, and lung. The genome, we identified four introns, but there is no transcript of a completely different, including the tyrosine kinase domain. For recombinant outer FGFR5β5γ region to produce a non-membrane protein, was cloned in frame with the Fc fragment of human lgG1. Instead of the FGF-2 ligand and recombinant FGFR5βFcR5γFc, and showed specific binding to EGF or FGF-7,. However, biological data indicates that FGF-2 binding to these proteins at lower affinity FGFR2C of the receptor analogs. The above data indicate that this receptor should be considered as the first member of the family of FGFR.

New fibroblast growth factor receptor as defined in FGFR5 (FGFR) is identified by the EST database lymph node stromal cell cDNA library of mouse. And has an identity of about 32% of the extracellular domain of FGFR1-4 in EST. Library screening with this EST was identified alternative transcripts of two functions identified as FGFR5γ and FGFR5β we. The main difference between these transcripts whereas that contain only one FGFR5γ2, its FGFR5β, extracellular Ig domain contains three. It is that unique features of FGFR5, the intracellular tyrosine kinase domain that does not contain it. The predicted structure modeling of the extracellular domain of FGFR5γ, he suggests that it was a member of a subset of the I set of Ig superfamily of FGFR dove consistency known. Northern analysis of mouse and human showed that FGFR5 mRNA is detected in a wide range of tissues, including kidney, brain, and lung. The genome, we identified four introns, but there is no transcript of a completely different, including the tyrosine kinase domain. For recombinant outer FGFR5β5γ region to produce a non-membrane protein, was cloned in frame with the Fc fragment of human lgG1. Instead of the FGF-2 ligand and recombinant FGFR5βFcR5γFc, and showed specific binding to EGF or FGF-7,. However, biological data indicates that FGF-2 binding to these proteins at lower affinity FGFR2C of the receptor analogs. The above data indicate that this receptor should be considered as the first member of the family of FGFR.

for members (FGFR5), fibroblast growth factor receptor (FGFR) family of the fibroblast growth factor 5, fibroblast growth factor receptor-like amino acids are evolutionarily conserved and highly member between 1 (FGFRL1) which is known as a receptor. Immunoglobulin-like domains of the three transmembrane segments of the hydrophobic agent and the full-length protein is composed of an extracellular region consisting of the cytoplasmic tyrosine kinase domain. Trigger a cascade of downstream signals affect the differentiation and mitosis Finally, the extracellular portion of the protein is reacted with fibroblast growth factor. It is that unique features of FGFRL1/FGFR5, the intracellular tyrosine kinase domain that does not contain it. Such as the diaphragm and muscles of the tongue, depending on the type of muscle, and relatively high FGFRL1/FGFR5 especially. As well as hands and feet, contrast (brain, lung, liver, kidney, intestine) of, only Fgfrl1 baseline manifested by skeletal muscle and heart organs of many other. FGFRL1/FGFR5 includes, FGFR the other are represented by the muscles and cartilage to modulate FGF signaling probably interact.

Similar to the murine fibroblast growth factor receptor 1, FGFRL1 protein 1, and 5, FGFR5 fibroblast growth factor FGF receptor-like, known as receptors for single-pass type I membrane protein. FGFR5 is expressed in the pancreas and cartilage tissue mainly. Is expressed liver, kidney, heart, skeletal muscle and in the brain very, it is expressed lung, intestine, spleen weak. The FGFR5, (immunoglobulin-like) domain contains C2 type Ig-like three. It is that unique features of FGFR5, the intracellular tyrosine kinase domain that does not contain it. Mammals, including humans and mice, have a copy of the gene but FGFRL1, fish, have a copy FGFRL1a FGFRL1b and at least two. That their receptors fibroblast growth factor (FGF) is a major effect on intracellular signaling control embryogenesis are known. I have an adverse effect on cell proliferation FGFR5. Detected in fetal 7, it becomes clearly visible on day 11, and increased to day 17 at first. FGFR5 is able to act as a decoy receptor for FGF ligand.