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- Table of Contents
Facts about Vasoactive intestinal polypeptide receptor 1.
This is a receptor for VIP.
The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.The affinity is VIP = PACAP-27 > PACAP-38. .
Human | |
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Gene Name: | VIPR1 |
Uniprot: | P32241 |
Entrez: | 7433 |
Belongs to: |
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G-protein coupled receptor 2 family |
FLJ41949; HVR1; II; PACAP type II receptor; PACAP-R2; RDC1; type II; V1RG; vasoactive intestinal peptide receptor 1; vasoactive intestinal polypeptide receptor 1; VIP R1; VIP receptor, type I; VIPR; VIPR1; VPAC1; VPAC1R
Mass (kDA):
51.547 kDA
Human | |
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Location: | 3p22.1 |
Sequence: | 3; NC_000003.12 (42489299..42537573) |
In lung, HT-29 colonic epithelial cells, Raji B-lymphoblasts. Lesser extent in brain, heart, kidney, liver and placenta. Not expressed in CD4+ or CD8+ T-cells. Expressed in the T-cell lines HARRIS, HuT 78, Jurkat and SUP-T1, but not in the T- cell lines Peer, MOLT-4, HSB and YT.
Cell membrane; Multi-pass membrane protein.
The VIPR1 gene encodes the precursor of hMPV F, and is also found in the GP160-based SSM. It can be used for identifying a variety of viruses. This article will focus on its most important uses in biotechnological science. The GP160 ectodomain is one of the most commonly used viral sequences in biotech research.
Syncytium formation requires the presence of an N-glycosylation spot in the HMPVF precursor. This can be identified using a novel protein–protein interaction. It is predicted that N-glycosylation sites will reduce fusion. The function of the G proteins in paramyxovirus membranefusion is not yet understood. Paramyxovirus infection requires that the protein be cleaved. It appears that the predicted cleavage site is correct.
The human metapneumovirus, also known as HMPV, has been recently identified and is associated with severe breathing disorders. Molecular diagnostic testing has raised public awareness about the virus' potential to cause infection. The virus's genome remains poorly understood and it is not known what its genetic diversity looks like. It is not clear whether the virus is endemic or common in different parts.
The VIPR1 marker is used for hMPMV F precursor. This marker can be used in order to identify a subset mutations. The F gene is highly conserved and has a 99% identity rate within the UK. However, the G gene is a complex component. It only shares 53% of its amino acids with the other groups. The best uses for the VIPR1 marker to hMPVF precursor are not yet known.
The MARV GP ectodomain has two types: EBOV or cleaved. Both have a mucine-like domain. EBOV GPs lack a missing GP2-wing. These proteins were characterized using trypsin cleavage. If R2 values were high enough, the 1:1 model was used to fit the curves.
These antibodies recognized a single HCDR3 Loop that is located in the MARV GP ectodomain. The full-length native Ab heavy-chain encodes the 17-residue loop HCDR3 that recognizes MARV GP. Scientists were able discover the specific mechanisms of these interactions thanks to the structure of HCDR3-loop binding site.
Different epitopes in the MARV GP could overlap and compete with one another. However, the MARV GP may have multiple epitopes. Antibodies that recognize these different epitopes could result in specific binding. These epitopes have been shown to be beneficial in the treatment of MARV. They could be used to make vaccines and immunogen containing compositions.
Recent research found that SARS-CoV in humans has two types SARS/CoV ectodomains. The SARS-CoV ectodomains can bind ACE2 type I integral membrane protein, but the human SARS-CoV can bind ACE2 palm civet ACE2. Adaptation to humans can be caused by mutations in the binding domain. These mutations have been associated wit enhanced virulence.
SARS CoV S ectodomains consist of two distinct domains. One is a N-terminal (NTD) domain and one is a receptor binding (RBD). These domains are essential for the virus’ entry into the host cell. SARS-CoV S ectodomains bind human angiotensin-converting enzyme 2 (ACE2), which is a cellular receptor.
These two types SARS-CoV Ectodomains share structural similarities with betacoronaviruses as well as wild-type SARS-CoV Ectodomains. The SARS CoV S2 Ectodomain has two helical components that interdigitate near the membrane-distal edge of the trimeric peak. The SARS-CoV S2 structure shows great conservation within coronavirus species, and the two types of SARS-CoV S prefusion strains are nearly identical across regions.
The SARS-CoV S ectodomain's two-dimensional structure is similar to wild-type S ectodomain. However, the SARS-CoV S1NTD is not well resolved in cryo-EM map and the structure has similar affinities for ACE2 receivers. The three-dimensional structures of SARS-CoV ectodomains were derived from crystallographic data, allowing scientists to analyze its structure more precisely.
The sequence for the RABV GP ectodomain is different from that for the Inf B HA predecessor. The sequence of Ectodomain (minus SP) is the main difference (SEQ ID Nr. 98). The sequence for the SP ectodomain, which is 59 amino-acids long, is the most conserved of all the RABV GP subtypes.
The sequence ID number is 88 in the ectodomain. It consists four homologous segments of approximately one hundred and seventy-eighty amino acids in length. These two regions are linked together by a cyclic nuclear nucleotide. The sequences genes of the ectodomains and the sequences of GP subtypes are closely related.
The RABV GP ectodomid, which is part of the HIV genome, is used as an antiviral agent. This agent is known as Ectodomain minus SP 20-650 and is currently available as a generic drug. It has many advantages over other antivirals. It is able to target RABV GP ectodomains.
The HA Subunit is found in HIV's GP ectodomain. It also contains D25 interaction domain (amino acid 61-97).
The ectodomain polypeptide of HIV and RABV can be artificially stabilized by coupling complementary heptad repeats to a structure-stabilizing moiety. The anti-parallel 2-helix bundle of heptad reprints prevents rearrangement.
The ectodomain polypeptide of the invention is constructed using knowledge of the location of a precursor protein. The precursor proteins include various functional and structural moiety domains. These precursor proteins include illustrative examples of ectodomain polypeptides. Furthermore, the ectodomain peptides of this invention are compatible with RABV GP160 fusion Protein.
This vaccine can block replication of the RABV GP ectodomain virus in a variety experimental models. A clinical trial has shown that RABV GP160-based SSM has a high rate of antiviral activity in vivo. The fusion protein was characterized by a series of experiments.
The VSV G epidomain was studied in detail using 16 Lyssavirus glycoproteins (precursors) to create multiple alignments. The AA within the ectodomain, AA 160 to168 and 181 to 180, 181 to 18,8 and AA 243-251 were selected for analysis. These proteins were similar to RVG at 65% identity.
An antibody against VSV G captured MLV Env viruses with high efficiency. This pairing was not as efficient as other pairs of glycoproteins actively recruited into viral assembly sites. However, it was still more efficient than straight infection. Its capture efficiency was five times higher than that of the uncoated control. However, this is not an absolute measure of viral capture efficiency. It is important to remember that co-packaging VSV–G or MLV Env viruses may prove more difficult than initially thought.
PMID: 8390245 by Sreedharan S.P., et al. Cloning and functional expression of a human neuroendocrine vasoactive intestinal peptide receptor.
PMID: 8179610 by Couvineau A., et al. Human intestinal VIP receptor: cloning and functional expression of two cDNA encoding proteins with different N-terminal domains.