PDBsum entry 3ewv

Calcium binding protein

PDB id: 3ewv

Contents

Protein chains

145 a.a. *

17 a.a. *

Metals

_CA ×4

Waters ×90

* Residue conservation analysis

PDB id:

3ewv

Name:

Calcium binding protein

Title:

Crystal structure of calmodulin complexed with a peptide

Structure:

Calmodulin. Chain: a. Synonym: cam. Engineered: yes. Tumor necrosis factor receptor superfamily member 16. Chain: e. Fragment: helix5 of death domain. Synonym: low-affinity nerve growth factor receptor, ngf receptor, gp80-lngfr, p75 icd, low affinity neurotrophin receptor p75ntr, cd271

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630. Other_details: this sequence occurs naturally in humans.

Resolution:

2.60Å R-factor: 0.231 R-free: 0.282

Authors:

T.Jiang,P.Cao,Y.Gong,H.J.Yu,W.J.Gui,W.T.Zhang

Key ref:

P.Cao et al. (2014). Structural insights into the mechanism of calmodulin binding to death receptors. Acta Crystallogr D Biol Crystallogr, 70, 1604-1613. PubMed id: 24914971 DOI: 10.1107/S1399004714006919

Date:

16-Oct-08 Release date: 20-Oct-09

Protein chain

P0DP23  (CALM1_HUMAN) -  Calmodulin-1 from Homo sapiens

Seq: 149 a.a.

Struc: 145 a.a.

Protein chain

P08138  (TNR16_HUMAN) -  Tumor necrosis factor receptor superfamily member 16 from Homo sapiens

Seq: 427 a.a.

Struc: 17 a.a.

DOI no: 10.1107/S1399004714006919

Acta Crystallogr D Biol Crystallogr 70:1604-1613 (2014)

PubMed id: 24914971

Structural insights into the mechanism of calmodulin binding to death receptors.

P.Cao, W.Zhang, W.Gui, Y.Dong, T.Jiang, Y.Gong.

ABSTRACT

The death receptors Fas, p75(NTR) and DR6 are key components of extrinsically activated apoptosis. Characterization of how they interact with the adaptors is crucial in order to unravel the signalling mechanisms. However, the exact conformation that their intracellular death domain adopts upon binding downstream partners remains unclear. One model suggests that it adopts a typical compact fold, whilst a second model proposed an open conformation. Calmodulin (CaM), a major calcium sensor, has previously been reported to be one of the Fas adaptors that modulate apoptosis. This work reports that CaM also binds directly to the death domains of p75(NTR) and DR6, indicating that it serves as a common modulator of the death receptors. Two crystal structures of CaM in complexes with the corresponding binding regions of Fas and p75(NTR) are also reported. Interestingly, the precise CaM-binding sites were mapped to different regions: helix 1 in Fas and helix 5 in p75(NTR) and DR6. A novel 1-11 motif for CaM binding was observed in p75(NTR). Modelling the complexes of CaM with full-length receptors reveals that the opening of the death domains would be essential in order to expose their binding sites for CaM. These results may facilitate understanding of the diverse functional repertoire of death receptors and CaM and provide further insights necessary for the design of potential therapeutic peptide agents.