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PDBsum entry 1iq3

Go to PDB code: 
protein metals links
Endocytosis/exocytosis PDB id
1iq3
Jmol
Contents
Protein chain
110 a.a. *
Metals
_CA
* Residue conservation analysis
PDB id:
1iq3
Name: Endocytosis/exocytosis
Title: Solution structure of the eps15 homology domain of a human pob1
Structure: Ralbp1-interacting protein (partner of ralbp1). Chain: a. Fragment: eh domain(residues 126-228). Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 18 models
Authors: S.Koshiba,T.Kigawa,J.Iwahara,A.Kikuchi,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref:
S.Koshiba et al. (1999). Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1). FEBS Lett, 442, 138-142. PubMed id: 9928989 DOI: 10.1016/S0014-5793(98)01644-5
Date:
06-Jun-01     Release date:   27-Jun-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8NFH8  (REPS2_HUMAN) -  RalBP1-associated Eps domain-containing protein 2
Seq:
Struc:
 
Seq:
Struc:
660 a.a.
110 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

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

 

 
DOI no: 10.1016/S0014-5793(98)01644-5 FEBS Lett 442:138-142 (1999)
PubMed id: 9928989  
 
 
Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1).
S.Koshiba, T.Kigawa, J.Iwahara, A.Kikuchi, S.Yokoyama.
 
  ABSTRACT  
 
The solution structure of the Eps15 homology (EH) domain of a human POB1 (partner of RaIBP1) has been determined by uniform 13C/15N labeling and heteronuclear multidimensional nuclear magnetic resonance spectroscopy. The POB1 EH domain consists of two EF-hand structures, and the second one binds a calcium ion. In the calcium-bound state, the orientation of the fourth alpha-helix relative to the other helices of the POB1 EH domain is slightly different from that of calbindin, and much more different from those of calmodulin and troponin C, on the basis of their atomic coordinates.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. ^1H-^15N HSQC NMR spectra of 0.6 mM of the uniformly ^15N-labeled POB1 EH domain with 3.0 mM CaCl[2], in the presence of (a) 0 mM EDTA and (b) 6.0 mM EDTA.
Figure 4.
Fig. 4. The distribution of the NOE contacts in the POB1 EH domain as a function of the sequence position. Inter- and intraresidue NOEs are shown as open and filled boxes, respectively.
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (1999, 442, 138-142) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
18983828 S.S.Singhal, S.Yadav, C.Roth, and J.Singhal (2009).
RLIP76: A novel glutathione-conjugate and multi-drug transporter.
  Biochem Pharmacol, 77, 761-769.  
18200045 J.Rumpf, B.Simon, N.Jung, T.Maritzen, V.Haucke, M.Sattler, and Y.Groemping (2008).
Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity.
  EMBO J, 27, 558-569.
PDB code: 2jxc
18154663 E.Santonico, S.Panni, M.Falconi, L.Castagnoli, and G.Cesareni (2007).
Binding to DPF-motif by the POB1 EH domain is responsible for POB1-Eps15 interaction.
  BMC Biochem, 8, 29.  
15386349 R.Sharma, S.S.Singhal, D.Wickramarachchi, Y.C.Awasthi, and S.Awasthi (2004).
RLIP76 (RALBP1)-mediated transport of leukotriene C4 (LTC4) in cancer cells: implications in drug resistance.
  Int J Cancer, 112, 934-942.  
12866021 S.Awasthi, S.S.Singhal, R.Sharma, P.Zimniak, and Y.C.Awasthi (2003).
Transport of glutathione conjugates and chemotherapeutic drugs by RLIP76 (RALBP1): a novel link between G-protein and tyrosine kinase signaling and drug resistance.
  Int J Cancer, 106, 635-646.  
11389591 S.Kim, D.N.Cullis, L.A.Feig, and J.D.Baleja (2001).
Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences.
  Biochemistry, 40, 6776-6785.
PDB code: 1fi6
10873829 D.J.Owen, and J.P.Luzio (2000).
Structural insights into clathrin-mediated endocytosis.
  Curr Opin Cell Biol, 12, 467-474.  
10757979 J.L.Enmon, T.de Beer, and M.Overduin (2000).
Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites.
  Biochemistry, 39, 4309-4319.
PDB code: 1c07
  11206052 Y.Kuroda, K.Tani, Y.Matsuo, and S.Yokoyama (2000).
Automated search of natively folded protein fragments for high-throughput structure determination in structural genomics.
  Protein Sci, 9, 2313-2321.  
10471276 B.Whitehead, M.Tessari, A.Carotenuto, P.M.van Bergen en Henegouwen, and G.W.Vuister (1999).
The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins.
  Biochemistry, 38, 11271-11277.
PDB code: 1qjt
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.