1UUJ
N-terminal domain of Lissencephaly-1 protein (Lis-1)
Summary for 1UUJ
| Entry DOI | 10.2210/pdb1uuj/pdb |
| Descriptor | PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB ALPHA SUBUNIT, SULFATE ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | platelet-activating factor acetylhydrolase, mitosis, neurogenesis, cytoskeleton, cell division, microtubule |
| Biological source | MUS MUSCULUS (MOUSE) |
| Total number of polymer chains | 4 |
| Total formula weight | 41654.03 |
| Authors | Cooper, D.R.,Kim, M.H.,Devedjiev, Y.,Derewenda, U.,Derewenda, Z.S. (deposition date: 2003-12-22, release date: 2004-07-29, Last modification date: 2024-10-23) |
| Primary citation | Kim, M.H.,Cooper, D.R.,Oleksy, A.,Devedjiev, Y.,Derewenda, U.,Reiner, O.,Otlewski, J.,Derewenda, Z.S. The Structure of the N-Terminal Domain of the Product of the Lissencephaly Gene Lis1 and its Functional Implications Structure, 12:987-, 2004 Cited by PubMed Abstract: 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. PubMed: 15274919DOI: 10.1016/J.STR.2004.03.024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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