1eyh: Difference between revisions

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<StructureSection load='1eyh' size='340' side='right'caption='[[1eyh]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
<StructureSection load='1eyh' size='340' side='right'caption='[[1eyh]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1eyh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EYH FirstGlance]. <br>
<table><tr><td colspan='2'>[[1eyh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYH FirstGlance]. <br>
</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=1eyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyh OCA], [http://pdbe.org/1eyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eyh RCSB], [http://www.ebi.ac.uk/pdbsum/1eyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyh ProSAT]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyh OCA], [https://pdbe.org/1eyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyh RCSB], [https://www.ebi.ac.uk/pdbsum/1eyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>   
[[https://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eyh ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eyh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Epsin|Epsin]]
== References ==
== References ==
<references/>
<references/>

Revision as of 09:33, 11 August 2021

CRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTIONCRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTION

Structural highlights

1eyh is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EPN1_RAT] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.[1] [2] [3]

Evolutionary Conservation

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

See Also

References

  1. ↑ Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH, Di Fiore PP, De Camilli P. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature. 1998 Aug 20;394(6695):793-7. PMID:9723620 doi:http://dx.doi.org/10.1038/29555
  2. ↑ Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science. 2001 Feb 9;291(5506):1047-51. PMID:11161217 doi:http://dx.doi.org/10.1126/science.291.5506.1047
  3. ↑ Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT. Curvature of clathrin-coated pits driven by epsin. Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027 doi:10.1038/nature01020

1eyh, resolution 1.56Å

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