This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2kgl

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 11:12, 25 December 2014

NMR solution structure of MESD

Structural highlights

2kgl is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Mesdc2 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[MESD2_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

How the endoplasmic reticulum (ER) folding machinery coordinates general and specialized chaperones during protein translation and folding remains an important unanswered question. Here, we show two structural domains in MESD, a specialized chaperone for LRP5/6, carry out dual functions. The chaperone domain forms a complex with the immature receptor, maintaining the beta-propeller (BP) domain in an interaction competent state for epidermal growth factor-repeat binding. This promotes proper folding of the BP domain, causing a binding switch from the chaperone domain to the escort domain. The escort complex ensures LRP5/6 safe-trafficking from the ER to the Golgi by preventing premature ligand-binding. Inside the Golgi, the BP domain may contain a histidine switch, regulating MESD dissociation and retrieval. Together, we generate a plausible cell biology picture of the MESD/LRP5/6 pathway, suggesting that it is the specialized chaperones, MESD, that serves as the folding template to drive proper folding and safe trafficking of large multidomain proteins LRP5/6.

Two Structural and Functional Domains of MESD Required for Proper Folding and Trafficking of LRP5/6.,Chen J, Liu CC, Li Q, Nowak C, Bu G, Wang J Structure. 2011 Mar 9;19(3):313-23. PMID:21397183^[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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kgl"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kgl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kgl RCSB], [http://www.ebi.ac.uk/pdbsum/2kgl PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MESD2_MOUSE MESD2_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.<ref>PMID:12581525</ref> <ref>PMID:21397183</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2kgl

From Proteopedia

Revision as of 11:12, 25 December 2014

NMR solution structure of MESD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox