1gjj
From Proteopedia
(New page: 200px<br /> <applet load="1gjj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gjj" /> '''N-TERMINAL CONSTANT REGION OF THE NUCLEAR E...) |
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'''N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2'''<br /> | '''N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The nuclear envelope proteins LAP2, emerin and MAN1 share a conserved | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1GJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cai, M.]] | [[Category: Cai, M.]] | ||
| - | [[Category: Clore, G | + | [[Category: Clore, G M.]] |
[[Category: inner nuclear membrane protein]] | [[Category: inner nuclear membrane protein]] | ||
[[Category: lamin-associated polypeptide]] | [[Category: lamin-associated polypeptide]] | ||
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[[Category: multidimensional nmr dipolar couplings]] | [[Category: multidimensional nmr dipolar couplings]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:45 2008'' |
Revision as of 10:50, 21 February 2008
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N-TERMINAL CONSTANT REGION OF THE NUCLEAR ENVELOPE PROTEIN LAP2
Contents |
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.
Disease
Known disease associated with this structure: Cardiomyopathy, dilated, 1T OMIM:[188380]
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
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