1y76
From Proteopedia
(New page: 200px<br /> <applet load="1y76" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y76" /> '''Solution Structure of Patj/Pals1 L27 Domain...) |
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'''Solution Structure of Patj/Pals1 L27 Domain Complex'''<br /> | '''Solution Structure of Patj/Pals1 L27 Domain Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Initially identified in Caenorhabditis elegans Lin-2 and Lin-7, L27 domain | + | Initially identified in Caenorhabditis elegans Lin-2 and Lin-7, L27 domain is a protein-protein interaction domain capable of organizing scaffold proteins into supramolecular assemblies by formation of heteromeric L27 domain complexes. L27 domain-mediated protein assemblies have been shown to play essential roles in cellular processes including asymmetric cell division, establishment and maintenance of cell polarity, and clustering of receptors and ion channels. The structural basis of L27 domain heteromeric complex assembly is controversial. We determined the high-resolution solution structure of the prototype L27 domain complex formed by mLin-2 and mLin-7 as well as the solution structure of the L27 domain complex formed by Patj and Pals1. The structures suggest that a tetrameric structure composed of two units of heterodimer is a general assembly mode for cognate pairs of L27 domains. Structural analysis of the L27 domain complex structures further showed that the central four-helix bundles mediating tetramer assembly are highly distinct between different pairs of L27 domain complexes. Biochemical studies revealed that the C-terminal alpha-helix responsible for the formation of the central helix bundle is a critical specificity determinant for each L27 domain in choosing its binding partner. Our results provide a unified picture for L27 domain-mediated protein-protein interactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y76 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1Y76 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y76 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Feng, W.]] | [[Category: Feng, W.]] | ||
| - | [[Category: Long, J | + | [[Category: Long, J F.]] |
[[Category: Zhang, M.]] | [[Category: Zhang, M.]] | ||
[[Category: cell polarity]] | [[Category: cell polarity]] | ||
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[[Category: scaffold protein]] | [[Category: scaffold protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:25 2008'' |
Revision as of 14:02, 21 February 2008
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Solution Structure of Patj/Pals1 L27 Domain Complex
Overview
Initially identified in Caenorhabditis elegans Lin-2 and Lin-7, L27 domain is a protein-protein interaction domain capable of organizing scaffold proteins into supramolecular assemblies by formation of heteromeric L27 domain complexes. L27 domain-mediated protein assemblies have been shown to play essential roles in cellular processes including asymmetric cell division, establishment and maintenance of cell polarity, and clustering of receptors and ion channels. The structural basis of L27 domain heteromeric complex assembly is controversial. We determined the high-resolution solution structure of the prototype L27 domain complex formed by mLin-2 and mLin-7 as well as the solution structure of the L27 domain complex formed by Patj and Pals1. The structures suggest that a tetrameric structure composed of two units of heterodimer is a general assembly mode for cognate pairs of L27 domains. Structural analysis of the L27 domain complex structures further showed that the central four-helix bundles mediating tetramer assembly are highly distinct between different pairs of L27 domain complexes. Biochemical studies revealed that the C-terminal alpha-helix responsible for the formation of the central helix bundle is a critical specificity determinant for each L27 domain in choosing its binding partner. Our results provide a unified picture for L27 domain-mediated protein-protein interactions.
About this Structure
1Y76 is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins., Feng W, Long JF, Zhang M, Proc Natl Acad Sci U S A. 2005 May 10;102(19):6861-6. Epub 2005 Apr 29. PMID:15863617
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