In molecular biology, the lamprin family of proteins consists of several lamprin proteins from the Sea lamprey Petromyzon marinus. Lamprin, an insoluble non-collagen, non-elastin protein, is the major connective tissue component of the fibrillar extracellular matrix of lamprey annular cartilage.

Lamprin
Identifiers
SymbolLamprin
PfamPF06403
InterProIPR009437
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Although not generally homologous to any other protein, soluble lamprins contain a tandemly repeated peptide sequence (GGLGY), which is present in both silk moth chorion proteins and spider dragline silk. Strong homologies to this repeat sequence are also present in several mammalian and avian elastins. It is thought that these proteins share a structural motif which promotes self-aggregation and fibril formation in proteins through interdigitation of hydrophobic side chains in beta-sheet/beta-turn structures, a motif that has been preserved in recognisable form over several hundred million years of evolution.[1]

References

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  1. ^ Robson P, Wright GM, Sitarz E, Maiti A, Rawat M, Youson JH, Keeley FW (January 1993). "Characterization of lamprin, an unusual matrix protein from lamprey cartilage. Implications for evolution, structure, and assembly of elastin and other fibrillar proteins". J. Biol. Chem. 268 (2): 1440–7. doi:10.1016/S0021-9258(18)54095-3. PMID 7678258.

Further reading

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This article incorporates text from the public domain Pfam and InterPro: IPR009437