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PDBsum entry 2kfh

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protein metals Protein-protein interface(s) links
Protein binding PDB id
2kfh
Jmol
Contents
Protein chains
105 a.a. *
12 a.a. *
Metals
_CA
* Residue conservation analysis
PDB id:
2kfh
Name: Protein binding
Title: Structure of thE C-terminal domain of ehd1 with fnyestgpftak
Structure: Eh domain-containing protein 1. Chain: a. Fragment: eh domain, residues 435-534. Synonym: testilin, hpast1. Engineered: yes. Rab11-fip2 gpf peptide fnyestgpftak. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ehd1, past, past1, cdabp0131. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide has been synthesized chemically
NMR struc: 10 models
Authors: F.Kieken,M.Jovic,M.Tonelli,N.Naslavsky,S.Caplan,P.Sorgen
Key ref: F.Kieken et al. (2009). Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1. Protein Sci, 18, 2471-2479. PubMed id: 19798736
Date:
20-Feb-09     Release date:   22-Dec-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9H4M9  (EHD1_HUMAN) -  EH domain-containing protein 1
Seq:
Struc:
 
Seq:
Struc:
534 a.a.
105 a.a.*
Protein chain
No UniProt id for this chain
Struc: 12 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  

 

 
Protein Sci 18:2471-2479 (2009)
PubMed id: 19798736  
 
 
Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.
F.Kieken, M.Jović, M.Tonelli, N.Naslavsky, S.Caplan, P.L.Sorgen.
 
  ABSTRACT  
 
Eps15 homology (EH)-domain containing proteins are regulators of endocytic membrane trafficking. EH-domain binding to proteins containing the tripeptide NPF has been well characterized, but recent studies have shown that EH-domains are also able to interact with ligands containing DPF or GPF motifs. We demonstrate that the three motifs interact in a similar way with the EH-domain of EHD1, with the NPF motif having the highest affinity due to the presence of an intermolecular hydrogen bond. The weaker affinity for the DPF and GPF motifs suggests that if complex formation occurs in vivo, they may require high ligand concentrations, the presence of successive motifs and/or specific flanking residues.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21067929 N.Naslavsky, and S.Caplan (2011).
EHD proteins: key conductors of endocytic transport.
  Trends Cell Biol, 21, 122-131.  
20106972 F.Kieken, M.Sharma, M.Jovic, S.S.Giridharan, N.Naslavsky, S.Caplan, and P.L.Sorgen (2010).
Mechanism for the selective interaction of C-terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners.
  J Biol Chem, 285, 8687-8694.
PDB code: 2ksp
20329706 G.D.Henry, D.J.Corrigan, J.V.Dineen, and J.D.Baleja (2010).
Charge effects in the selection of NPF motifs by the EH domain of EHD1.
  Biochemistry, 49, 3381-3392.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.