PDBsum entry: 3dit

Signaling protein

PDB id: 3dit

Contents

Protein chains

186 a.a. *

Waters ×90

* Residue conservation analysis

PDB id:

3dit

Name:

Signaling protein

Title:

Crystal structure of mad mh2 domain

Structure:

Protein mothers against dpp. Chain: a, b, c. Fragment: mad mh2 domain. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: mad, cg12399. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.20Å R-factor: 0.244 R-free: 0.310

Authors:

R.Hao,J.W.Wu,Z.X.Wang

Key ref:

R.Hao et al. (2008). Structure of Drosophila Mad MH2 domain. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 986-990. PubMed id: 18997322 Ref: Full text

Date:

20-Jun-08 Release date: 12-May-09

Protein chains

P42003  (MAD_DROME) -  Protein mothers against dpp

Seq: 455 a.a.

Struc: 186 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)
• Biological process: regulation of transcription, DNA-dependent (1 term)

Full text	Acta Crystallogr Sect F Struct Biol Cryst Commun 64:986-990 (2008)
PubMed id: 18997322

Structure of Drosophila Mad MH2 domain.

R.Hao, L.Chen, J.W.Wu, Z.X.Wang.

ABSTRACT

In Drosophila, decapentaplegic (Dpp), a member of the TGF-beta superfamily, plays a pivotal role in control of proliferation, global patterning and induction of specific cell fates. Together with Medea, mother against Dpp (Mad), the founding member of the Smad family, specifically transduces the Dpp signal from the plasma membrane to the nucleus. Here, the crystal structure of the MH2 domain of Mad, which closely matches those of other Smad MH2 domains, is reported at 3.2 A resolution. The conservation of Smad protein structures is consistent with their evolutionary conserved and significant function. Furthermore, sequence alignment revealed that most of the variant amino acids in Smad proteins specific to the BMP pathway (Smad1, Smad5 and Mad) were clustered at the surface. In particular, Ser296 and Asp297 of Mad introduced a negative patch into the positive surface observed in the surface electrostatic potential of Smad1 MH2.