3TAD: Liprin-alpha/Liprin-beta complex

Crystal Structure of the Liprin-alpha/Liprin-beta complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 12 Oct 2011.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Homo sapiens, Mus musculus
Chains: 4
Atoms: 8,163
Mol. weight: 129.77 kDa
Released: 12 Oct 2011

Explore 3TAD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3TAD contains 90 α-helices and 12 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 24 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	872-889	18
α-helix	895-897	3
β-strand	899	1	1
α-helix	900-909	10
α-helix	915-924	10
β-strand	927	1	1
α-helix	928-933	6
α-helix	936-938	3
α-helix	939-943	5
α-helix	948-964	17
α-helix	1021-1023	3
α-helix	1024-1028	5
α-helix	1029-1031	3
α-helix	1035-1037	3
α-helix	1038-1043	6
α-helix	1048-1051	4
α-helix	1056-1057	2
α-helix	1058-1062	5
α-helix	1068-1083	16
α-helix	1088-1097	10
α-helix	1110-1119	10
α-helix	1123-1126	4
α-helix	1127-1129	3
α-helix	1136-1141	6
α-helix	1147-1153	7
α-helix	1161-1176	16

Chain B: 24 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	873-889	17
α-helix	895-897	3
β-strand	899	1	2
α-helix	900-909	10
α-helix	915-924	10
β-strand	927	1	2
α-helix	928-932	5
α-helix	936-938	3
α-helix	939-943	5
α-helix	948-964	17
α-helix	1021-1023	3
α-helix	1024-1028	5
α-helix	1029-1031	3
α-helix	1035-1037	3
α-helix	1038-1043	6
α-helix	1048-1051	4
α-helix	1056-1057	2
α-helix	1058-1062	5
α-helix	1068-1083	16
α-helix	1088-1096	9
α-helix	1110-1118	9
α-helix	1123-1126	4
α-helix	1127-1129	3
α-helix	1136-1141	6
α-helix	1147-1153	7
α-helix	1161-1176	16

Chain C: 21 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	603-605	3
α-helix	608-617	10
α-helix	624-627	4
α-helix	635-639	5
α-helix	642-648	7
α-helix	654-669	16
α-helix	675-677	3
α-helix	680-690	11
α-helix	693-695	3
α-helix	696-702	7
α-helix	706-710	5
β-strand	713	1	3
α-helix	714-719	6
β-strand	724	1	4
α-helix	725-740	16
α-helix	755-757	3
α-helix	760-765	6
α-helix	768-777	10
α-helix	784-787	4
α-helix	794-799	6
α-helix	805-811	7
α-helix	819-833	15
α-helix	835-844	10
β-strand	850	1	5

Chain D: 21 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	603-605	3
β-strand	607	1	6
α-helix	608-615	8
α-helix	616-620	5
α-helix	621-623	3
α-helix	624-627	4
β-strand	633	1	6
α-helix	634-639	6
α-helix	642-648	7
α-helix	654-668	15
α-helix	675-677	3
α-helix	680-690	11
α-helix	693-695	3
α-helix	696-702	7
α-helix	706-710	5
β-strand	713	1	5
α-helix	714-719	6
β-strand	724	1	4
α-helix	725-740	16
α-helix	760-763	4
α-helix	768-777	10
α-helix	784-787	4
α-helix	794-799	6
α-helix	805-811	7
α-helix	819-845	27
β-strand	850	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Liprin-alpha-2	A, B	protein	297	Homo sapiens	O75334 (AlphaFold model)
Liprin-beta-1	C, D	protein	265	Mus musculus	Q8C8U0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3TAD_1 Liprin-alpha-2 (chains A, B)
GPGSEFGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVA
ACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTTLAY
GDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQY
GIMCLKRLNYDRKELERRREASQHEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHG
SLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLLALGTERRLDESDDKNFRR

Sequence of entity 2 (C, D), FASTA

>3TAD_2 Liprin-beta-1 (chains C, D)
GPGSGQSNSDLDMPFAKWTKEQVCSWLAEQGLGSYLSSGKHWIISGQTLLQASQQDLEKE
LGIKHSLHRKKLQLALQALGSEEETNYGKLDFNWVTRWLDDIGLPQYKTQFDEGRVDGRM
LHYMTVDDLLSLKVVSVLHHLSIKRAIQVLRINNFEPNCLRRRPSDENSITPSEVQQWTN
HRVMEWLRSVDLAEYAPNLRGSGVHGGLMVLEPRFNVETMAQLLNIPPNKTLLRRHLATH
FNLLIGAEAQHQKRDAMELPDYVLL

Primary citation

Liprin-mediated large signaling complex organization revealed by the liprin-alpha/CASK and liprin-alpha/liprin-beta complex structures. Wei, Z., Zheng, S., Spangler, S.A. et al. Mol Cell (2011) 43:586-598. DOI 10.1016/j.molcel.2011.07.021 · PubMed

Other PDB entries of the same protein (UniProt O75334 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7D2E 1.7 Å, Tetrameric coiled-coil structure of liprin-alpha2_H3
7D2G 1.7 Å, Coiled-coil structure of liprin-alpha2_H2delC
6IUH 1.8 Å, Crystal structure of GIT1 PBD domain in complex with Liprin-alpha2
3TAC 2.2 Å, Crystal Structure of the Liprin-alpha/CASK complex
7D2H 2.2 Å, Tetrameric coiled-coil structure of liprin-alpha2_H2
8Z22 2.75 Å, Crystal structure of the liprin-alpha2/RIM1 complex

Browse structure collections

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