ML domain

ML domain
X-ray structure of Der p 2, the major house dust mite allergen
Identifiers
Symbol	E1_DerP2_DerF2
Pfam	PF02221
InterPro	IPR003172
SCOP2	1a9v / SCOPe / SUPFAM
OPM superfamily	91
OPM protein	1nep
CDD	cd00912
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

The MD-2-related lipid-recognition (ML) domain is implicated in lipid recognition, particularly in the recognition of pathogen related products. It has an immunoglobulin-like beta-sandwich fold similar to that of immunoglobulin E-set domains. This domain is present in the following proteins:

• Epididymal secretory protein E1 (also known as Niemann-Pick C2 protein), which is known to bind cholesterol. Niemann-Pick disease type C2 is a fatal hereditary disease characterised by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. ^[1]
• House dust mite allergen proteins such as Der f 2 from Dermatophagoides farinae and Der p 2 from Dermatophagoides pteronyssinus . ^[2]

Human proteins containing this domain

LY86; LY96; MMD-1;

References

1. Lobel P, Stock AM, Friedland N, Liou HL (2003). "Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2512–2517. Bibcode:2003PNAS..100.2512F. doi: 10.1073/pnas.0437840100 . PMC   151372 . PMID   12591954.
2. Kristensen O, Kastrup JS, Skov LK, Gajhede M, Larsen JN, Johannessen BR, Bolwig C, Spangfort M, Lund K (2005). "Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity". FEBS Lett. 579 (5): 1208–12. Bibcode:2005FEBSL.579.1208J. doi: 10.1016/j.febslet.2004.11.115 . PMID   15710415. S2CID   30079878.

This article incorporates text from the public domain Pfam and InterPro: IPR003172