2i9s

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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. 2007 Mar 7;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17342452 17342452]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17342452 17342452]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ferredoxin-like-fold]]
[[Category: ferredoxin-like-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:22:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:23 2008''

Revision as of 15:50, 21 February 2008


2i9s

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The solution structure of the core of mesoderm development (MESD).

Overview

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.

About this Structure

2I9S is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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