2bqq: Difference between revisions
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[[Image:2bqq.gif|left|200px]] | [[Image:2bqq.gif|left|200px]] | ||
'''X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN''' | {{Structure | ||
|PDB= 2bqq |SIZE=350|CAPTION= <scene name='initialview01'>2bqq</scene>, resolution 2.200Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BQQ is a [ | 2BQQ 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=2BQQ OCA]. | ||
==Reference== | ==Reference== | ||
The DC-module of doublecortin: dynamics, domain boundaries, and functional implications., Cierpicki T, Kim MH, Cooper DR, Derewenda U, Bushweller JH, Derewenda ZS, Proteins. 2006 Sep 1;64(4):874-82. PMID:[http:// | The DC-module of doublecortin: dynamics, domain boundaries, and functional implications., Cierpicki T, Kim MH, Cooper DR, Derewenda U, Bushweller JH, Derewenda ZS, Proteins. 2006 Sep 1;64(4):874-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16835924 16835924] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin-like fold]] | [[Category: ubiquitin-like fold]] | ||
''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 16:05:26 2008'' | ||
Revision as of 17:05, 20 March 2008
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X-RAY STRUCURE OF THE N-TERMINAL DOMAIN OF HUMAN DOUBLECORTIN
OverviewOverview
The doublecortin-like (DC) domains, which usually occur in tandem, constitute novel microtubule-binding modules. They were first identified in doublecortin (DCX), a protein expressed in migrating neurons, and in the doublecortin-like kinase (DCLK). They are also found in other proteins, including the RP1 gene product which-when mutated-causes a form of inherited blindness. We previously reported an X-ray structure of the N-terminal DC domain of DCLK (N-DCLK), and a solution structure of an analogous module of human doublecortin (N-DCX). These studies showed that the DC domain has a tertiary fold closely reminiscent of ubiquitin and similar to several GTPase-binding domains. We now report an X-ray structure of a mutant of N-DCX, in which the C-terminal fragment (residues 139-147) unexpectedly shows an altered, "open" conformation. However, heteronuclear NMR data show that this C-terminal fragment is only transiently open in solution, and assumes a predominantly "closed" conformation. While the "open" conformation may be artificially stabilized by crystal packing interactions, the observed switching between the "open" and "closed" conformations, which shortens the linker between the two DC-domains by approximately 20 A, is likely to be of functional importance in the control of tubulin polymerization and microtubule bundling by doublecortin.
DiseaseDisease
Known diseases associated with this structure: Lissencephaly, X-linked OMIM:[300121], Subcortical laminal heteropia, X-linked OMIM:[300121]
About this StructureAbout this Structure
2BQQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The DC-module of doublecortin: dynamics, domain boundaries, and functional implications., Cierpicki T, Kim MH, Cooper DR, Derewenda U, Bushweller JH, Derewenda ZS, Proteins. 2006 Sep 1;64(4):874-82. PMID:16835924
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