1H9F
LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN LAP2
Summary for 1H9F
| Entry DOI | 10.2210/pdb1h9f/pdb |
| Related | 1H9E |
| NMR Information | BMRB: 5043 |
| Descriptor | Lamina-associated polypeptide 2, isoform alpha (1 entity in total) |
| Functional Keywords | membrane protein, inner nuclear membrane protein, lamina-associated polypeptide, emerin, lem domain |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 6543.31 |
| Authors | Laguri, C.,Gilquin, B.,Wolff, N.,Romi-Lebrun, R.,Courchay, K.,Callebaut, I.,Worman, H.J.,Zinn-Justin, S. (deposition date: 2001-03-09, release date: 2001-06-17, Last modification date: 2024-05-15) |
| Primary citation | Laguri, C.,Gilquin, B.,Wolff, N.,Romi-Lebrun, R.,Courchay, K.,Callebaut, I.,Worman, H.J.,Zinn-Justin, S. Structural Characterization of the Lem Motif Common to Three Human Inner Nuclear Membrane Proteins Structure, 9:503-, 2001 Cited by PubMed Abstract: Integral membrane proteins of the inner nuclear membrane are involved in chromatin organization and postmitotic reassembly of the nucleus. The discovery that mutations in the gene encoding emerin causes X-linked Emery-Dreifuss muscular dystrophy has enhanced interest in such proteins. A common structural domain of 50 residues, called the LEM domain, has been identified in emerin MAN1, and lamina-associated polypeptide (LAP) 2. In particular, all LAP2 isoforms share an N-terminal segment composed of such a LEM domain that is connected to a highly divergent LEM-like domain by a linker that is probably unstructured. PubMed: 11435115DOI: 10.1016/S0969-2126(01)00611-6 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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