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2kfg

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Revision as of 11:10, 18 July 2018

Structure of the C-terminal domain of EHD1 in complex with FNYESTDPFTAK

Structural highlights

2kfg is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2kff, 2kfh
Gene:	EHD1, PAST, PAST1, CDABP0131 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EHD1_HUMAN] Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.,Kieken F, Jovic M, Tonelli M, Naslavsky N, Caplan S, Sorgen PL Protein Sci. 2009 Dec;18(12):2471-9. PMID:19798736^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Naslavsky N, Boehm M, Backlund PS Jr, Caplan S. Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane. Mol Biol Cell. 2004 May;15(5):2410-22. Epub 2004 Mar 12. PMID:15020713 doi:http://dx.doi.org/10.1091/mbc.E03-10-0733
↑ George M, Ying G, Rainey MA, Solomon A, Parikh PT, Gao Q, Band V, Band H. Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans. BMC Cell Biol. 2007 Jan 18;8:3. PMID:17233914 doi:http://dx.doi.org/10.1186/1471-2121-8-3
↑ Kieken F, Jovic M, Tonelli M, Naslavsky N, Caplan S, Sorgen PL. Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1. Protein Sci. 2009 Dec;18(12):2471-9. PMID:19798736 doi:10.1002/pro.258

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kfg"

@@ Line 1: / Line 1: @@
 ==Structure of the C-terminal domain of EHD1 in complex with FNYESTDPFTAK==
 <StructureSection load='2kfg' size='340' side='right' caption='[[2kfg]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kff|2kff]], [[2kfh|2kfh]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHD1, PAST, PAST1, CDABP0131 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfg OCA], [http://pdbe.org/2kfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kfg RCSB], [http://www.ebi.ac.uk/pdbsum/2kfg PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kfg OCA], [http://pdbe.org/2kfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kfg RCSB], [http://www.ebi.ac.uk/pdbsum/2kfg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kfg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/2kfg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/2kfg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 40: / Line 41: @@
 [[Category: Sorgen, P]]
 [[Category: Tonelli, M]]
+[[Category: Calcium]]
 [[Category: Cell membrane]]
+[[Category: Coiled coil]]
 [[Category: Ehd1]]
 [[Category: Endosome]]

2kfg

From Proteopedia

Revision as of 11:10, 18 July 2018

Structure of the C-terminal domain of EHD1 in complex with FNYESTDPFTAK

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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