1uuj
From Proteopedia
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|PDB= 1uuj |SIZE=350|CAPTION= <scene name='initialview01'>1uuj</scene>, resolution 1.75Å | |PDB= 1uuj |SIZE=350|CAPTION= <scene name='initialview01'>1uuj</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Bez+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Bez+Binding+Site+For+Chain+C'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uuj OCA], [http://www.ebi.ac.uk/pdbsum/1uuj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uuj RCSB]</span> | ||
}} | }} | ||
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[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Kim, M H.]] | [[Category: Kim, M H.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: BEZ]] | ||
| - | [[Category: SO4]] | ||
[[Category: cell division]] | [[Category: cell division]] | ||
[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
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[[Category: platelet-activating factor acetylhydrolase]] | [[Category: platelet-activating factor acetylhydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:15:29 2008'' |
Revision as of 21:15, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-TERMINAL DOMAIN OF LISSENCEPHALY-1 PROTEIN (LIS-1)
Overview
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 Structure
1UUJ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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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