1h9f
From Proteopedia
|
LEM DOMAIN OF HUMAN INNER NUCLEAR MEMBRANE PROTEIN LAP2
Contents |
Overview
BACKGROUND: 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., RESULTS: We have determined the three-dimensional structures of the LEM, and LEM-like domains of LAP2 using nuclear magnetic resonance and, molecular modeling. Both domains adopt the same fold, mainly composed of, two large parallel alpha helices. CONCLUSIONS: The structural LEM motif is, found in human inner nuclear membrane proteins and in protein-protein, interaction domains from bacterial multienzyme complexes. This suggests, that LEM and LEM-like domains are protein-protein interaction domains. A, region conserved in all LEM domains, at the surface of helix 2, could, mediate interaction between LEM domains and a common protein partner.
Disease
Known disease associated with this structure: Cardiomyopathy, dilated, 1T OMIM:[188380]
About this Structure
1H9F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural characterization of the LEM motif common to three human inner nuclear membrane proteins., Laguri C, Gilquin B, Wolff N, Romi-Lebrun R, Courchay K, Callebaut I, Worman HJ, Zinn-Justin S, Structure. 2001 Jun;9(6):503-11. PMID:11435115
Page seeded by OCA on Mon Nov 12 17:14:21 2007
