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 | ||||||||
| SCOP | 1a9v | ||||||||
| SUPERFAMILY | 1a9v | ||||||||
| OPM protein | 1nep | ||||||||
| CDD | cd00912 | ||||||||
| |||||||||
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
- ↑ 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): –. doi:10.1073/pnas.0437840100. PMC 151372. PMID 12591954.
- ↑ 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. doi:10.1016/j.febslet.2004.11.115. PMID 15710415.
This article incorporates text from the public domain Pfam and InterPro IPR003172
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