1ijx
From Proteopedia
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|PDB= 1ijx |SIZE=350|CAPTION= <scene name='initialview01'>1ijx</scene>, resolution 1.9Å | |PDB= 1ijx |SIZE=350|CAPTION= <scene name='initialview01'>1ijx</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SFRP-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= SFRP-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ijy|1IJY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ijx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ijx OCA], [http://www.ebi.ac.uk/pdbsum/1ijx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ijx RCSB]</span> | ||
}} | }} | ||
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[[Category: Rattner, A.]] | [[Category: Rattner, A.]] | ||
[[Category: Sharma, D.]] | [[Category: Sharma, D.]] | ||
| - | [[Category: SO4]] | ||
[[Category: cysteine-rich]] | [[Category: cysteine-rich]] | ||
[[Category: frizzled protein structure]] | [[Category: frizzled protein structure]] | ||
[[Category: wnt receptor]] | [[Category: wnt receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:48 2008'' |
Revision as of 18:20, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SFRP-3 (Mus musculus) | ||||||
| Related: | 1IJY
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF SECRETED FRIZZLED-RELATED PROTEIN 3 (SFRP-3;FZB)
Overview
Members of the Frizzled family of seven-pass transmembrane proteins serve as receptors for Wnt signalling proteins. Wnt proteins have important roles in the differentiation and patterning of diverse tissues during animal development, and inappropriate activation of Wnt signalling pathways is a key feature of many cancers. An extracellular cysteine-rich domain (CRD) at the amino terminus of Frizzled proteins binds Wnt proteins, as do homologous domains in soluble proteins-termed secreted Frizzled-related proteins-that function as antagonists of Wnt signalling. Recently, an LDL-receptor-related protein has been shown to function as a co-receptor for Wnt proteins and to bind to a Frizzled CRD in a Wnt-dependent manner. To investigate the molecular nature of the Wnt signalling complex, we determined the crystal structures of the CRDs from mouse Frizzled 8 and secreted Frizzled-related protein 3. Here we show a previously unknown protein fold, and the design and interpretation of CRD mutations that identify a Wnt-binding site. CRDs exhibit a conserved dimer interface that may be a feature of Wnt signalling. This work provides a framework for studies of homologous CRDs in proteins including muscle-specific kinase and Smoothened, a component of the Hedgehog signalling pathway.
About this Structure
1IJX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains., Dann CE, Hsieh JC, Rattner A, Sharma D, Nathans J, Leahy DJ, Nature. 2001 Jul 5;412(6842):86-90. PMID:11452312
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