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3  structures 76  species 0  interactions 147  sequences 21  architectures

Family: L27_1 (PF09058)

Summary: L27_1

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This is the Wikipedia entry entitled "L27 domain". More...

L27 domain Edit Wikipedia article

L27 domain
PDB 1rso EBI.jpg
Structure of presynaptic protein SAP97.[1]
Identifiers
Symbol L27
Pfam PF02828
InterPro IPR014775
L27_1
PDB 1rso EBI.jpg
hetero-tetrameric l27 (lin-2, lin-7) domain complexes as organization platforms of supra-molecular assemblies
Identifiers
Symbol L27_1
Pfam PF09058
InterPro IPR015143
L27_2
PDB 1vf6 EBI.jpg
2.1 angstrom crystal structure of the pals-1-l27n and patj l27 heterodimer complex
Identifiers
Symbol L27_2
Pfam PF09045
InterPro IPR015132
L27_N
PDB 1vf6 EBI.jpg
2.1 angstrom crystal structure of the pals-1-l27n and patj l27 heterodimer complex
Identifiers
Symbol L27_N
Pfam PF09060
InterPro IPR015145

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]

References[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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. 

Further reading[edit]

  • 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


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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 Provide feedback

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

  1. 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 EPMC:15048107

  2. 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 EPMC:17237226


External database links

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

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Alignments

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  Seed
(4)
Full
(147)
Representative proteomes NCBI
(170)
Meta
(0)
RP15
(24)
RP35
(30)
RP55
(48)
RP75
(67)
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  Seed
(4)
Full
(147)
Representative proteomes NCBI
(170)
Meta
(0)
RP15
(24)
RP35
(30)
RP55
(48)
RP75
(67)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Curation and family details

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Seed source: pdb_1rso
Previous IDs: none
Type: Domain
Author: Mistry J, Sammut SJ
Number in seed: 4
Number in full: 147
Average length of the domain: 59.10 aa
Average identity of full alignment: 57 %
Average coverage of the sequence by the domain: 8.95 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.6 21.6
Trusted cut-off 21.6 23.0
Noise cut-off 20.6 21.3
Model length: 64
Family (HMM) version: 5
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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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