2I9S
The solution structure of the core of mesoderm development (MESD).
Summary for 2I9S
| Entry DOI | 10.2210/pdb2i9s/pdb |
| Descriptor | Mesoderm development candidate 2 (1 entity in total) |
| Functional Keywords | ferredoxin-like-fold, chaperone |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Endoplasmic reticulum: Q9ERE7 |
| Total number of polymer chains | 1 |
| Total formula weight | 10956.52 |
| Authors | Koehler, C.,Andersen, O.,Diehl, A.,Schmieder, P.,Krause, G.,Oschkinat, H. (deposition date: 2006-09-06, release date: 2007-05-01, Last modification date: 2024-05-29) |
| Primary citation | Kohler, C.,Andersen, O.M.,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.GENOM., 7:131-138, 2006 Cited by PubMed Abstract: 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. PubMed: 17342452DOI: 10.1007/s10969-007-9016-5 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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