Lipocalin

Retinol-binding protein in a calculated membrane-bound state of the protein 1kt6
Identifiers
SymbolLipocalin
PfamPF00061
Pfam clanCL0116
ECOD9.1.1
InterProIPR000566
PROSITEPDOC00187
SCOP21hms / SCOPe / SUPFAM
OPM superfamily50
OPM protein1kt6
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Lipocalin-like domain
Structure of the Escherichia coli lipocalin.[1]
Identifiers
SymbolLipocalin_2
PfamPF08212
Pfam clanCL0116
InterProIPR013208
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids, and most lipocalins are also able to bind to complexed iron (via siderophores[2] or flavonoids[3]) as well as heme.[4] They share limited regions of sequence homology and a common tertiary structure architecture.[5][6][7][8][9] This is an eight stranded antiparallel beta barrel with a repeated + 1 topology enclosing an internal ligand binding site.[7][8]

These proteins are found in gram negative bacteria, vertebrate cells, and invertebrate cells, and in plants. Lipocalins have been associated with many biological processes, among them immune response, pheromone transport, biological prostaglandin synthesis, retinoid binding, and cancer cell interactions.[10]

  1. ^ Campanacci V, Nurizzo D, Spinelli S, Valencia C, Tegoni M, Cambillau C (March 2004). "The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding". FEBS Letters. 562 (1–3): 183–188. Bibcode:2004FEBSL.562..183C. doi:10.1016/S0014-5793(04)00199-1. PMID 15044022. S2CID 26737744.
  2. ^ Goetz DH, Holmes MA, Borregaard N, Bluhm ME, Raymond KN, Strong RK (November 2002). "The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition". Molecular Cell. 10 (5): 1033–1043. doi:10.1016/s1097-2765(02)00708-6. PMID 12453412.
  3. ^ Roth-Walter F, Pacios LF, Bianchini R, Jensen-Jarolim E (December 2017). "Linking iron-deficiency with allergy: role of molecular allergens and the microbiome". Metallomics. 9 (12): 1676–1692. doi:10.1039/c7mt00241f. PMID 29120476.
  4. ^ Matz JM, Drepper B, Blum TB, van Genderen E, Burrell A, Martin P, et al. (July 2020). "A lipocalin mediates unidirectional heme biomineralization in malaria parasites". Proceedings of the National Academy of Sciences of the United States of America. 117 (28): 16546–16556. Bibcode:2020PNAS..11716546M. doi:10.1073/pnas.2001153117. PMC 7368307. PMID 32601225.
  5. ^ Pervaiz S, Brew K (September 1987). "Homology and structure-function correlations between alpha 1-acid glycoprotein and serum retinol-binding protein and its relatives". FASEB Journal. 1 (3): 209–214. doi:10.1096/fasebj.1.3.3622999. PMID 3622999. S2CID 12416282.
  6. ^ Igarashi M, Nagata A, Toh H, Urade Y, Hayaishi O (June 1992). "Structural organization of the gene for prostaglandin D synthase in the rat brain". Proceedings of the National Academy of Sciences of the United States of America. 89 (12): 5376–5380. Bibcode:1992PNAS...89.5376I. doi:10.1073/pnas.89.12.5376. PMC 49294. PMID 1608945.
  7. ^ a b Cowan SW, Newcomer ME, Jones TA (1990). "Crystallographic refinement of human serum retinol binding protein at 2A resolution". Proteins. 8 (1): 44–61. doi:10.1002/prot.340080108. PMID 2217163. S2CID 21613341.
  8. ^ a b Flower DR, North AC, Attwood TK (May 1993). "Structure and sequence relationships in the lipocalins and related proteins". Protein Science. 2 (5): 753–761. doi:10.1002/pro.5560020507. PMC 2142497. PMID 7684291.
  9. ^ Godovac-Zimmermann J (February 1988). "The structural motif of beta-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules?". Trends in Biochemical Sciences. 13 (2): 64–66. doi:10.1016/0968-0004(88)90031-X. PMID 3238752.
  10. ^ Araos P, Amador CA (2022). "Neutrophil gelatinase-associated lipocalin as an immunomodulator in endocrine hypertension". Front Endocrinol (Lausanne). 13: 1006790. doi:10.3389/fendo.2022.1006790. PMC 9640732. PMID 36387895.