Summary: L27_1
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This is the Wikipedia entry entitled "L27 domain". More...
L27 domain
| Structure of presynaptic protein SAP97.[1] | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | L27 | ||||||||
| Pfam | PF02828 | ||||||||
| InterPro | IPR014775 | ||||||||
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| hetero-tetrameric l27 (lin-2, lin-7) domain complexes as organization platforms of supra-molecular assemblies | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | L27_1 | ||||||||
| Pfam | PF09058 | ||||||||
| InterPro | IPR015143 | ||||||||
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| 2.1 angstrom crystal structure of the pals-1-l27n and patj l27 heterodimer complex | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | L27_2 | ||||||||
| Pfam | PF09045 | ||||||||
| InterPro | IPR015132 | ||||||||
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| 2.1 angstrom crystal structure of the pals-1-l27n and patj l27 heterodimer complex | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | L27_N | ||||||||
| Pfam | PF09060 | ||||||||
| InterPro | IPR015145 | ||||||||
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The L27 domain is a protein domain that is found in receptor targeting proteins Lin-2 and Lin-7 (LIN7A, LIN7B, LIN7C), as well as some protein kinases and human MPP2 protein.[2] The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three alpha-helices.[1]
The L27_2 domain is a protein-protein interaction domain capable of organising scaffold proteins into supramolecular assemblies by formation of heteromeric L27_2 domain complexes. L27_2 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. Members of this family form specific heterotetrameric complexes, in which each domain contains three alpha-helices. The two N-terminal helices of each L27_2 domain pack together to form a tight, four-helix bundle in the heterodimer, whilst the third helix of each L27_2 domain forms another four-helix bundle that assembles the two units of the heterodimer into a tetramer.[3]
The L27_N domain is often found at the N-terminus of the L27 domain. It plays a role in the biogenesis of tight junctions and in the establishment of cell polarity in epithelial cells. Each L27_N domain consists of three alpha-helices, the first two of which form an antiparallel coiled-coil. Two L27 domains come together to form a four-helical bundle with the antiparallel coiled-coils formed by the first two helices. The third helix of each domain forms another coiled-coil packing at one end of the four-helix bundle, creating a large hydrophobic interface: the hydrophobic interactions are the major force that drives heterodimer formation.[4]
[edit] References
- ^ a b Feng W, Long JF, Fan JS, Suetake T, Zhang M (May 2004). "The tetrameric L27 domain complex as an organization platform for supramolecular assemblies". Nat. Struct. Mol. Biol. 11 (5): 475–80. doi:10.1038/nsmb751. PMID 15048107.
- ^ Doerks T, Bork P, Kamberov E, Makarova O, Muecke S, Margolis B (July 2000). "L27, a novel heterodimerization domain in receptor targeting proteins Lin-2 and Lin-7". Trends Biochem. Sci. 25 (7): 317–8. PMID 10871881.
- ^ Feng W, Long JF, Zhang M (May 2005). "A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins". Proc. Natl. Acad. Sci. U.S.A. 102 (19): 6861–6. doi:10.1073/pnas.0409346102. PMC 1100767. PMID 15863617. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1100767.
- ^ Li Y, Karnak D, Demeler B, Margolis B, Lavie A (July 2004). "Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes". EMBO J. 23 (14): 2723–33. doi:10.1038/sj.emboj.7600294. PMC 514954. PMID 15241471. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514954.
[edit] Further Reading
- Petrosky KY, Ou HD, Löhr F, Dötsch V, Lim WA (November 2005). "A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes". J. Biol. Chem. 280 (46): 38528–36. doi:10.1074/jbc.M506536200. PMID 16147993.
This article incorporates text from the public domain Pfam and InterPro IPR014775
This article incorporates text from the public domain Pfam and InterPro IPR015143
This article incorporates text from the public domain Pfam and InterPro IPR015132
This article incorporates text from the public domain Pfam and InterPro IPR015145
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
L27_1
The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three alpha-helices [1].
Literature references
-
Feng W, Long JF, Fan JS, Suetake T, Zhang M; , Nat Struct Mol Biol. 2004;11:475-480.: The tetrameric L27 domain complex as an organization platform for supramolecular assemblies. PUBMED:15048107
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Bohl J, Brimer N, Lyons C, Vande Pol SB; , J Biol Chem. 2007;282:9392-9400.: The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions. PUBMED:17237226
External database links
| PANDIT: | PF09058 |
| Pseudofam: | PF09058 |
| SYSTERS: | L27_1 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR015143
The L27 domain is a protein interaction module that exists in a large family of scaffold proteins, functioning as an organisation centre of large protein assemblies required for the establishment and maintenance of cell polarity. L27 domains form specific heterotetrameric complexes, in which each domain contains three alpha-helices [PUBMED:15048107].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
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Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | pdb_1rso |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mistry J, Sammut SJ |
| Number in seed: | 4 |
| Number in full: | 80 |
| Average length of the domain: | 60.50 aa |
| Average identity of full alignment: | 57 % |
| Average coverage of the sequence by the domain: | 10.98 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 64 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the L27_1 domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence