2BAP: Diaphanous protein homolog 1

Crystal structure of the N-terminal mDia1 Armadillo Repeat Region and Dimerisation Domain in complex with the mDia1 autoregulatory domain (DAD). Determined by X-ray diffraction at 3.3 Å resolution. Released 7 Mar 2006.

Method: X-ray diffraction
Resolution: 3.3 Å
Organism: Mus musculus
Chains: 4
Atoms: 4,960
Mol. weight: 85.99 kDa
Released: 7 Mar 2006

Explore 2BAP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BAP contains 38 α-helices and 0 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: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	137-144	8
α-helix	151-164	14
α-helix	169-191	23
α-helix	202-216	15
α-helix	219-227	9
α-helix	231-238	8
α-helix	244-258	15
α-helix	266-280	15
α-helix	287-291	5
α-helix	299-311	13
α-helix	319-332	14
α-helix	334-337	4
α-helix	340-343	4
α-helix	349-351	3
α-helix	353-377	25
α-helix	381-391	11
α-helix	398-408	11
α-helix	418-433	16

Chain B: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	137-144	8
α-helix	151-165	15
α-helix	168-192	25
α-helix	203-215	13
α-helix	219-225	7
α-helix	231-236	6
α-helix	244-259	16
α-helix	266-280	15
α-helix	287-291	5
α-helix	302-313	12
α-helix	319-330	12
α-helix	334-338	5
α-helix	340-343	4
α-helix	347-376	30
α-helix	382-387	6
α-helix	388-392	5
α-helix	398-408	11
α-helix	418-433	16

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1184-1190	7

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1182-1190	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Diaphanous protein homolog 1	A, B	protein	317	Mus musculus	O08808 (AlphaFold model)
Diaphanous protein homolog 1	C, D	protein	56	Mus musculus	O08808 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2BAP_1 Diaphanous protein homolog 1 (chains A, B)
SAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKE
ETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLL
SALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALIT
PAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDI
RMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVL
HKNGTDPDFKCRHLQID

Sequence of entity 2 (C, D), FASTA

>2BAP_2 Diaphanous protein homolog 1 (chains C, D)
MRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRG

Primary citation

The regulation of mDia1 by autoinhibition and its release by Rho*GTP. Lammers, M., Rose, R., Scrima, A. et al. EMBO J (2005) 24:4176-4187. DOI 10.1038/sj.emboj.7600879 · 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
4UWX 1.65 Å, Structure of liprin-alpha3 in complex with mDia1 Diaphanous- inhibitory domain
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
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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