PDBsum entry 3a98

Signaling protein

PDB id: 3a98

Contents

Protein chains

157 a.a. *

190 a.a. *

167 a.a. *

Waters ×133

* Residue conservation analysis

PDB id:

3a98

Name:

Signaling protein

Title:

Crystal structure of the complex of the interacting regions of dock2 and elmo1

Structure:

Dedicator of cytokinesis protein 2. Chain: a, c. Fragment: n-terminal domains, sh3 domain, residues 1-177. Synonym: dock2. Engineered: yes. Engulfment and cell motility protein 1. Chain: b, d. Fragment: c-terminal domains, ph domain, residues 532-727. Synonym: elmo1, ced-12 homolog.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dock2, kiaa0209. Expressed in: cell free protein synthesis. Gene: elmo1, kiaa0281.

Resolution:

2.10Å R-factor: 0.226 R-free: 0.268

Authors:

K.Hanawa-Suetsugu,M.Kukimoto-Niino,S.Sekine,T.Ito,C.Mishima- Tsumagari,T.Terada,M.Shirouzu,Y.Fukui,S.Yokoyama

Key ref:

K.Hanawa-Suetsugu et al. (2012). Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms. Proc Natl Acad Sci U S A, 109, 3305-3310. PubMed id: 22331897

Date:

21-Oct-09 Release date: 27-Oct-10

Protein chains

Q92608  (DOCK2_HUMAN) -  Dedicator of cytokinesis protein 2 from Homo sapiens

Seq: 1830 a.a.

Struc: 157 a.a.

Protein chain

Q92556  (ELMO1_HUMAN) -  Engulfment and cell motility protein 1 from Homo sapiens

Seq: 727 a.a.

Struc: 190 a.a.*

Protein chain

Q92556  (ELMO1_HUMAN) -  Engulfment and cell motility protein 1 from Homo sapiens

Seq: 727 a.a.

Struc: 167 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Proc Natl Acad Sci U S A 109:3305-3310 (2012)

PubMed id: 22331897

Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms.

K.Hanawa-Suetsugu, M.Kukimoto-Niino, C.Mishima-Tsumagari, R.Akasaka, N.Ohsawa, S.Sekine, T.Ito, N.Tochio, S.Koshiba, T.Kigawa, T.Terada, M.Shirouzu, A.Nishikimi, T.Uruno, T.Katakai, T.Kinashi, D.Kohda, Y.Fukui, S.Yokoyama.

ABSTRACT

No abstract given.