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1mfw
From Proteopedia
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|PDB= 1mfw |SIZE=350|CAPTION= <scene name='initialview01'>1mfw</scene>, resolution 1.600Å | |PDB= 1mfw |SIZE=350|CAPTION= <scene name='initialview01'>1mfw</scene>, resolution 1.600Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1mg4|1MG4]], [[1mjd|1MJD]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mfw OCA], [http://www.ebi.ac.uk/pdbsum/1mfw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mfw RCSB]</span> | ||
}} | }} | ||
| Line 33: | Line 36: | ||
[[Category: Otlewski, J.]] | [[Category: Otlewski, J.]] | ||
[[Category: Walsh, C A.]] | [[Category: Walsh, C A.]] | ||
| - | [[Category: SO4]] | ||
[[Category: cortex development]] | [[Category: cortex development]] | ||
[[Category: doublecortin]] | [[Category: doublecortin]] | ||
| Line 40: | Line 42: | ||
[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''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 22:15:40 2008'' |
Revision as of 19:15, 30 March 2008
| |||||||
| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1MG4, 1MJD
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN
Overview
The doublecortin-like domains (DCX), which typically occur in tandem, are novel microtubule-binding modules. DCX tandems are found in doublecortin, a 360-residue protein expressed in migrating neurons; the doublecortin-like kinase (DCLK); the product of the RP1 gene that is responsible for a form of inherited blindness; and several other proteins. Mutations in the gene encoding doublecortin cause lissencephaly in males and the 'double-cortex syndrome' in females. We here report a solution structure of the N-terminal DCX domain of human doublecortin and a 1.5 A resolution crystal structure of the equivalent domain from human DCLK. Both show a stable, ubiquitin-like tertiary fold with distinct structural similarities to GTPase-binding domains. We also show that the C-terminal DCX domains of both proteins are only partially folded. In functional assays, the N-terminal DCX domain of doublecortin binds only to assembled microtubules, whereas the C-terminal domain binds to both microtubules and unpolymerized tubulin.
About this Structure
1MFW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The DCX-domain tandems of doublecortin and doublecortin-like kinase., Kim MH, Cierpicki T, Derewenda U, Krowarsch D, Feng Y, Devedjiev Y, Dauter Z, Walsh CA, Otlewski J, Bushweller JH, Derewenda ZS, Nat Struct Biol. 2003 May;10(5):324-33. PMID:12692530
Page seeded by OCA on Sun Mar 30 22:15:40 2008
Categories: Homo sapiens | Single protein | Bushweller, J H. | Cierpickil, T. | Dauter, Z. | Derewenda, U. | Derewenda, Z. | Devedjiev, Y. | Feng, Y. | Kim, M H. | Krowarsch, D. | Otlewski, J. | Walsh, C A. | Cortex development | Doublecortin | Doublecortin-like kinase | Microtubule bundling | X-ray structure
