1uuj: Difference between revisions
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[[Image:1uuj.gif|left|200px]]<br /> | [[Image:1uuj.gif|left|200px]]<br /><applet load="1uuj" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1uuj" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1uuj, resolution 1.75Å" /> | caption="1uuj, resolution 1.75Å" /> | ||
'''N-TERMINAL DOMAIN OF LISSENCEPHALY-1 PROTEIN (LIS-1)'''<br /> | '''N-TERMINAL DOMAIN OF LISSENCEPHALY-1 PROTEIN (LIS-1)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1UUJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4, ACT and BEZ as [http://en.wikipedia.org/wiki/ligands ligands]. | 1UUJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4, ACT and BEZ as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Bez Binding Site For Chain C'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UUJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: platelet-activating factor acetylhydrolase]] | [[Category: platelet-activating factor acetylhydrolase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:12:33 2007'' | ||
Revision as of 19:02, 18 December 2007
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N-TERMINAL DOMAIN OF LISSENCEPHALY-1 PROTEIN (LIS-1)
OverviewOverview
Mutations in the Lis1 gene result in lissencephaly (smooth brain), a, debilitating developmental syndrome caused by the impaired ability of, postmitotic neurons to migrate to their correct destination in the, cerebral cortex. Sequence similarities suggest that the LIS1 protein, contains a C-terminal seven-blade beta-propeller domain, while the, structure of the N-terminal fragment includes the LisH (Lis-homology), motif, a pattern found in over 100 eukaryotic proteins with a hitherto, unknown function. We present the 1.75 A resolution crystal structure of, the N-terminal domain of mouse LIS1, and we show that the LisH motif is a, novel, thermodynamically very stable dimerization domain. The structure, explains the molecular basis of a low severity form of lissencephaly.
About this StructureAbout this Structure
1UUJ is a Single protein structure of sequence from Mus musculus with SO4, ACT and BEZ as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications., Kim MH, Cooper DR, Oleksy A, Devedjiev Y, Derewenda U, Reiner O, Otlewski J, Derewenda ZS, Structure. 2004 Jun;12(6):987-98. PMID:15274919
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