1mfw: Difference between revisions
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[[Image:1mfw.jpg|left|200px]] | [[Image:1mfw.jpg|left|200px]] | ||
'''STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN''' | {{Structure | ||
|PDB= 1mfw |SIZE=350|CAPTION= <scene name='initialview01'>1mfw</scene>, resolution 1.600Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MFW is a [ | 1MFW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFW OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12692530 12692530] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:43:02 2008'' | ||
Revision as of 13:43, 20 March 2008
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STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN
OverviewOverview
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 StructureAbout this Structure
1MFW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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