PDBsum entry 2lb2

Signaling protein/transcription

PDB id: 2lb2

Contents

Protein chains

35 a.a.

12 a.a.

PDB id:

2lb2

Name:

Signaling protein/transcription

Title:

Structure of the second domain of human nedd4l in complex with a phosphorylated ptpy motif derived from human smad3

Structure:

E3 ubiquitin-protein ligase nedd4-like. Chain: a. Fragment: residues 386-420. Synonym: nedd4.2, nedd4-2. Engineered: yes. Mothers against decapentaplegic homolog 3. Chain: b. Fragment: residues 178-189. Synonym: mad homolog 3, mad3, mothers against dpp homolog 3, hmad-3,

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: nedd4l, kiaa0439, nedl3. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606

NMR struc:

25 models

Authors:

M.J.Macias,E.Aragon,N.Goerner,A.Zaromytidou,Q.Xi,A.Escobedo, J.Massague

Key ref:

E.Aragón et al. (2011). A Smad action turnover switch operated by WW domain readers of a phosphoserine code. Genes Dev, 25, 1275-1288. PubMed id: 21685363

Date:

22-Mar-11 Release date: 06-Jul-11

Protein chain

Q96PU5  (NED4L_HUMAN) -  E3 ubiquitin-protein ligase NEDD4-like from Homo sapiens

Seq: 975 a.a.

Struc: 35 a.a.

Protein chain

P84022  (SMAD3_HUMAN) -  Mothers against decapentaplegic homolog 3 from Homo sapiens

Seq: 425 a.a.

Struc: 12 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.2.3.2.26 - HECT-type E3 ubiquitin transferase.
• Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine
• Enzyme class 2: Chain A: E.C.2.3.2.36 - RING-type E3 ubiquitin transferase (cysteine targeting).
• Reaction: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Genes Dev 25:1275-1288 (2011)

PubMed id: 21685363

A Smad action turnover switch operated by WW domain readers of a phosphoserine code.

E.Aragón, N.Goerner, A.I.Zaromytidou, Q.Xi, A.Escobedo, J.Massagué, M.J.Macias.

ABSTRACT

No abstract given.