Biology:Odorant-binding protein
| Pheromone/general odorant-binding protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | PBP_GOBP | ||||||||
| Pfam | PF01395 | ||||||||
| InterPro | IPR006170 | ||||||||
| SCOP2 | 1c3z / SCOPe / SUPFAM | ||||||||
| |||||||||
| odorant-binding protein 2A | |
|---|---|
 | |
| Identifiers | |
| Symbol | OBP2A |
| Alt. symbols | hOBPIIa, OBP |
| NCBI gene | 29991 |
| HGNC | 23380 |
| OMIM | 164320 |
| RefSeq | NM_014582 |
| UniProt | Q9NY56 |
| Other data | |
| Locus | Chr. 9 q34 |
| odorant-binding protein 2B | |
|---|---|
| Identifiers | |
| Symbol | OBP2B |
| Alt. symbols | hOBPIIb |
| NCBI gene | 29989 |
| HGNC | 23381 |
| OMIM | 604606 |
| RefSeq | NM_014581 |
| UniProt | Q9NPH6 |
| Other data | |
| Locus | Chr. 9 q34 |
Odorant-binding proteins are abundant small soluble proteins secreted in the nasal mucus of many animal species and in the sensillar lymph of chemosensory sensilla of insects.
The olfactory receptors of terrestrial animals exist in an aqueous environment, yet detect odorants that are primarily hydrophobic. The aqueous solubility of hydrophobic odorants is greatly enhanced via odorant-binding proteins, which exist in the extracellular fluid surrounding the odorant receptors.[1] This family is composed of pheromone binding proteins (PBP), which are male-specific and associate with pheromone-sensitive neurons and general-odorant-binding proteins (GOBP).
These proteins were initially identified on the basis of their ability to bind with moderate-affinity radioactively labeled odorants.[2][3]
References
- ↑ "Odorant-binding-protein subfamilies associate with distinct classes of olfactory receptor neurons in insects". J. Neurobiol. 22 (1): 74–84. 1991. doi:10.1002/neu.480220108. PMID 2010751.
- ↑ "Identification of a specific olfactory receptor for 2-isobutyl-3-methoxypyrazine". Biochem. J. 201 (1): 245–8. January 1982. PMID 7082286.
- ↑ PDB ID: 1CI0 W. Shi, D.A. Ostrov, S.E. Gerchman, V. Graziano, H. Kycia, B. Studier, S.C. Almo, S.K. Burley, New York Structural GenomiX Research Consortium (NYSGXRC). The Structure of PNP Oxidase from S. cerevisiae
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