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1mfw
From Proteopedia
(New page: 200px<br /> <applet load="1mfw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mfw, resolution 1.600Å" /> '''STRUCTURE OF N-TER...) |
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| - | [[Image:1mfw. | + | [[Image:1mfw.jpg|left|200px]]<br /><applet load="1mfw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mfw" size=" | + | |
caption="1mfw, resolution 1.600Å" /> | caption="1mfw, resolution 1.600Å" /> | ||
'''STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN'''<br /> | '''STRUCTURE OF N-TERMINAL DOUBLECORTIN DOMAIN FROM DCLK: SELENOMETHIONINE LABELED PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MFW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:24:04 2008'' |
Revision as of 14:24, 15 February 2008
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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 with as ligand. 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 Fri Feb 15 16:24:04 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. | SO4 | Cortex development | Doublecortin | Doublecortin-like kinase | Microtubule bundling | X-ray structure
