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1gjj

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjj OCA], [http://www.ebi.ac.uk/pdbsum/1gjj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gjj RCSB]</span>
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'''N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2'''
'''N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2'''
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[[Category: Cai, M.]]
[[Category: Cai, M.]]
[[Category: Clore, G M.]]
[[Category: Clore, G M.]]
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[[Category: inner nuclear membrane protein]]
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[[Category: Inner nuclear membrane protein]]
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[[Category: lamin-associated polypeptide]]
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[[Category: Lamin-associated polypeptide]]
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[[Category: lem domain]]
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[[Category: Lem domain]]
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[[Category: multidimensional nmr dipolar coupling]]
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[[Category: Multidimensional nmr dipolar coupling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:39:19 2008''
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Revision as of 14:39, 2 May 2008

Template:STRUCTURE 1gjj

N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2


Overview

The nuclear envelope proteins LAP2, emerin and MAN1 share a conserved approximately 40-residue 'LEM' motif. Loss of emerin causes Emery-Dreifuss muscular dystrophy. We have solved the solution NMR structure of the constant region of human LAP2 (residues 1-168). Human LAP2(1-168) has two structurally independent, non-interacting domains located at residues 1-50 ('LAP2-N') and residues 111-152 (LEM-domain), connected by an approximately 60-residue flexible linker. The two domains are structurally homologous, comprising a helical turn followed by two helices connected by an 11-12-residue loop. This motif is shared by subdomains of T4 endonuclease VII and transcription factor rho, despite negligible (< or =15%) sequence identity. NMR chemical shift mapping demonstrated that the LEM-domain binds BAF (barrier-to-autointegration factor), whereas LAP2-N binds DNA. Both binding surfaces comprise helix 1, the N-terminus of helix 2 and the inter-helical loop. Binding selectivity is determined by the nature of the surface residues in these binding sites, which are predominantly positively charged for LAP2-N and hydrophobic for the LEM-domain. Thus, LEM and LEM-like motifs form a common structure that evolution has customized for binding to BAF or DNA.

About this Structure

1GJJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA., Cai M, Huang Y, Ghirlando R, Wilson KL, Craigie R, Clore GM, EMBO J. 2001 Aug 15;20(16):4399-407. PMID:11500367 Page seeded by OCA on Fri May 2 17:39:19 2008

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