4UWX: Liprin-alpha3

Structure of liprin-alpha3 in complex with mDia1 Diaphanous- inhibitory domain. Determined by X-ray diffraction at 1.65 Å resolution. Released 6 May 2015.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: MUS MUSCULUS
Chains: 4
Atoms: 4,337
Mol. weight: 59.22 kDa
Ligands: 144, NI
Released: 6 May 2015

Explore 4UWX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4UWX contains 30 α-helices and 4 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: 14 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	133-143	11
α-helix	149-165	17
α-helix	168-191	24
α-helix	201-215	15
α-helix	219-226	8
α-helix	231-237	7
α-helix	244-258	15
α-helix	266-281	16
α-helix	287-292	6
β-strand	295	1	1
β-strand	297	1	1
α-helix	299-313	15
α-helix	319-329	11
α-helix	330-334	5
α-helix	335-342	8
α-helix	347-367	21

Chain B: 14 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	136-144	9
α-helix	149-165	17
α-helix	168-191	24
α-helix	201-215	15
α-helix	219-227	9
α-helix	231-237	7
α-helix	244-258	15
α-helix	266-281	16
α-helix	287-292	6
β-strand	295	1	2
β-strand	297	1	2
α-helix	299-313	15
α-helix	319-329	11
α-helix	330-334	5
α-helix	335-341	7
α-helix	347-368	22

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	568-580	13

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	568-581	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein diaphanous homolog 1	A, B	protein	239	MUS MUSCULUS	O08808 (AlphaFold model)
Liprin-alpha-3	C, D	protein	21	MUS MUSCULUS	P60469 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4UWX_1 PROTEIN DIAPHANOUS HOMOLOG 1 (chains A, B)
GSEFSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLH
DEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDA
AKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLIN
ALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKG

Sequence of entity 2 (C, D), FASTA

>4UWX_2 LIPRIN-ALPHA-3 (chains C, D)
TPRSARLERMAQALALQAGSP

Ligands and cofactors

ID	Name	Formula	Copies
144	Tris-hydroxymethyl-methyl-ammonium	C4 H12 N O3	2
NI	Nickel (II) ion	Ni	2

Primary citation

Structural and Biochemical Basis for the Inhibitory Effect of Liprin-Alpha3 on Mouse Diaphanous 1 (Mdia1) Function. Brenig, J., De Boor, S., Knyphausen, P. et al. J Biol Chem (2015) 290:14314. DOI 10.1074/JBC.M114.621946 · PubMed

Other PDB entries of the same protein (UniProt O08808 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2V8F 1.1 Å, Mouse Profilin IIa in complex with a double repeat from the FH1 domain of mDia1
2F31 2.1 Å, Crystal structure of the autoinhibitory switch in Formin mDia1; the DID/DAD complex
2BNX 2.4 Å, Crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin…
1V9D 2.6 Å, Crystal structure of the core FH2 domain of mouse mDia1
3EG5 2.7 Å, Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP
3OBV 2.75 Å, Autoinhibited Formin mDia1 Structure
1Z2C 3.0 Å, Crystal structure of mDIA1 GBD-FH3 in complex with RhoC-GMPPNP
3O4X 3.2 Å, Crystal structure of complex between amino and carboxy terminal fragments of mDia1
2BAP 3.3 Å, Crystal structure of the N-terminal mDia1 Armadillo Repeat Region and Dimerisation…
9B3D 3.41 Å, mDia1 in the middle of F-actin
8RU2 3.49 Å, Structure of the F-actin barbed end bound by formin mDia1
9B27 3.51 Å, Dia1 at the Barbed End of F-Actin

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