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Literature DB >> 17342452

The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.

Christian Köhler¹, Olav M Andersen, Annette Diehl, Gerd Krause, Peter Schmieder, Hartmut Oschkinat.

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.

Entities: Chemical

Mesh：

Substances：

Year: 2007 PMID： 17342452 DOI： 10.1007/s10969-007-9016-5

Source DB: PubMed Journal: J Struct Funct Genomics ISSN： 1345-711X

36 in total

1. An LDL-receptor-related protein mediates Wnt signalling in mice.

Authors: K I Pinson; J Brennan; S Monkley; B J Avery; W C Skarnes
Journal: Nature Date: 2000-09-28 Impact factor: 49.962

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3. Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.

Authors: Theresa A Ramelot; Shuisong Ni; Sharon Goldsmith-Fischman; John R Cort; Barry Honig; Michael A Kennedy
Journal: Protein Sci Date: 2003-07 Impact factor: 6.725

4. Rapid endocytosis of the low density lipoprotein receptor-related protein modulates cell surface distribution and processing of the beta-amyloid precursor protein.

Authors: Judy A Cam; Celina V Zerbinatti; Yonghe Li; Guojun Bu
Journal: J Biol Chem Date: 2005-02-10 Impact factor: 5.157

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Authors: R Koradi; M Billeter; K Wüthrich
Journal: J Mol Graph Date: 1996-02

6. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.

Authors: J Gitschier; B Moffat; D Reilly; W I Wood; W J Fairbrother
Journal: Nat Struct Biol Date: 1998-01

7. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.

Authors: R A Laskowski; J A Rullmannn; M W MacArthur; R Kaptein; J M Thornton
Journal: J Biomol NMR Date: 1996-12 Impact factor: 2.835

8. Six novel missense mutations in the LDL receptor-related protein 5 (LRP5) gene in different conditions with an increased bone density.

Authors: Liesbeth Van Wesenbeeck; Erna Cleiren; Jeppe Gram; Rodney K Beals; Olivier Bénichou; Domenico Scopelliti; Lyndon Key; Tara Renton; Cindy Bartels; Yaoqin Gong; Matthew L Warman; Marie-Christine De Vernejoul; Jens Bollerslev; Wim Van Hul
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9. An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.

Authors: T A Springer
Journal: J Mol Biol Date: 1998-11-06 Impact factor: 5.469

The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family.

1. An LDL-receptor-related protein mediates Wnt signalling in mice.

2. The Xplor-NIH NMR molecular structure determination package.

3. Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.

4. Rapid endocytosis of the low density lipoprotein receptor-related protein modulates cell surface distribution and processing of the beta-amyloid precursor protein.

5. MOLMOL: a program for display and analysis of macromolecular structures.

6. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.

7. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.

8. Six novel missense mutations in the LDL receptor-related protein 5 (LRP5) gene in different conditions with an increased bone density.

9. An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.

10. The genomics of disulfide bonding and protein stabilization in thermophiles.

1. NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.

2. Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type β propeller domains.

3. The structure of MESD45-184 brings light into the mechanism of LDLR family folding.

4. Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/6.

5. Cooperative folding and ligand-binding properties of LRP6 beta-propeller domains.