Neuropilin

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neuropilin 1
File:Neuropilin.png
Crystallographic structure of the dimeric B1 domain of human neuropilin 1.[1]
Identifiers
Symbol NRP1
Entrez 8829
HUGO 8004
OMIM 602069
PDB 3I97
RefSeq NM_001024628
UniProt O14786
Other data
Locus Chr. 10 p12
neuropilin 2
Identifiers
Symbol NRP2
Entrez 8828
HUGO 8005
OMIM 602070
RefSeq NM_201279
UniProt O60462
Other data
Locus Chr. 2 q34

Neuropilin is a protein receptor active in neurons.

There are two forms of Neuropilins, NRP-1 and NRP-2. They are transmembrane glycoproteins, and predominantly co-receptors for another class of proteins known as semaphorins. Of the semaphorins, NRP-1 and NRP-2 are specifically receptors for class-3 semaphorins, which, among many things, are responsible for axon guidance during the development of the nervous system in vertebrates.

Neuropilins work as co-receptors as they have a very small cytoplasmic domain and thus rely upon other molecules (normally plexins) to transduce their signals across a cell membrane. Neuropilins generally work as dimers and different combinations have different affinities for molecules. For example, NRP-1 homodimers have high affinity for Sema-3A, whilst NRP-2 homodimers have high affinity for Sema-3F.

Another ligand for neuropilins is VEGF, a growth factor involved in the regulation of angiogenesis.

Applications

Neuropilin-1 is a therapeutic target protein in the treatment for leukemia and lymphoma, since It has been shown that there is increased expression in neuropilin-1 in leukemia and lymphoma cell lines.[2] Also, antagonism of neuropilin-1 has been found to inhibit tumour cell migration and adhesion.[3]

Structure

Neuropilins contain the following four domains:

The structure of B1 domain (coagulation factor 5/8 type) of neuropilin-1 was determined through X-Ray Diffraction with a resolution of 2.90 Å. The secondary structure of this domain is 5% alpha helical and 46% beta sheet.[1]

Ramachandran plot.[4]

References

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External links

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