Structural highlights
Function
MESD_MOUSE Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mesoderm development (MESD) is a 224 amino acid mouse protein that acts as a molecular chaperone for receptors of the low-density lipoprotein receptor (LDLR) family. By recording (15)N-HSQC-NMR spectra of six different MESD constructs, we could determine a highly structured core region corresponding to residues 104-177. Here we firstly present the solution structure of this highly conserved core of MESD. It shows a four-stranded anti-parallel beta-sheet and two alpha-helices situated on one side of the sheet. Although described in the literature as structurally homologues to ferredoxins, the connectivity of secondary structure elements is different in the MESD fold. A structural comparison to entries of the PDB reveals a frequent domain with low sequence homology annotated as HMA and P-II domains in Pfam.
The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.,Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. Epub 2007 Mar 7. PMID:17342452[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hsieh JC, Lee L, Zhang L, Wefer S, Brown K, DeRossi C, Wines ME, Rosenquist T, Holdener BC. Mesd encodes an LRP5/6 chaperone essential for specification of mouse embryonic polarity. Cell. 2003 Feb 7;112(3):355-67. PMID:12581525
- ↑ Chen J, Liu CC, Li Q, Nowak C, Bu G, Wang J. Two Structural and Functional Domains of MESD Required for Proper Folding and Trafficking of LRP5/6. Structure. 2011 Mar 9;19(3):313-23. PMID:21397183 doi:10.1016/j.str.2011.01.010
- ↑ Kohler C, Andersen OM, Diehl A, Krause G, Schmieder P, Oschkinat H. The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family. J Struct Funct Genomics. 2006 Dec;7(3-4):131-8. Epub 2007 Mar 7. PMID:17342452 doi:10.1007/s10969-007-9016-5
