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PDBsum entry 2kfh
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Protein binding
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PDB id
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2kfh
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Contents |
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* Residue conservation analysis
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PDB id:
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Protein binding
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Title:
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Structure of thE C-terminal domain of ehd1 with fnyestgpftak
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Structure:
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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
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Source:
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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
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NMR struc:
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10 models
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Authors:
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F.Kieken,M.Jovic,M.Tonelli,N.Naslavsky,S.Caplan,P.Sorgen
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Key ref:
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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:
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Date:
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20-Feb-09
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Release date:
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22-Dec-09
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PROCHECK
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Headers
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References
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Enzyme class:
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Chain A:
E.C.?
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Protein Sci
18:2471-2479
(2009)
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PubMed id:
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Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.
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F.Kieken,
M.Jović,
M.Tonelli,
N.Naslavsky,
S.Caplan,
P.L.Sorgen.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Naslavsky,
and
S.Caplan
(2011).
EHD proteins: key conductors of endocytic transport.
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Trends Cell Biol,
21,
122-131.
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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.
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J Biol Chem,
285,
8687-8694.
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PDB code:
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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.
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Biochemistry,
49,
3381-3392.
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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.
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Links
