1inz

From Proteopedia

(Difference between revisions)

Current revision

SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN

Structural highlights

1inz is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

EPN1_HUMAN Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis.^[1]

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

Epsin is a protein that binds to the Eps15 homology (EH) domains, and is involved in clathrin-mediated endocytosis. The epsin N-terminal homology (ENTH) domain (about 140 amino acid residues) is well conserved in eukaryotes and is considered to be important for actin cytoskeleton organization in endocytosis. In this study, we have determined the solution structure of the ENTH domain (residues 1-144) of human epsin by multidimensional nuclear magnetic resonance spectroscopy. In the ENTH-domain structure, seven alpha-helices form a superhelical fold, consisting of two antiparallel two-helix HEAT motifs and one three-helix ARM motif, with a continuous hydrophobic core in the center. We conclude that the seven-helix superhelical fold defines the ENTH domain, and that the previously-reported eight-helix fold of a longer fragment of rat epsin 1 is divided into the authentic ENTH domain and a C-terminal flanking alpha-helix.

Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin.,Koshiba S, Kigawa T, Kikuchi A, Yokoyama S J Struct Funct Genomics. 2002;2(1):1-8. PMID:12836669^[2]

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

References

↑ Morinaka K, Koyama S, Nakashima S, Hinoi T, Okawa K, Iwamatsu A, Kikuchi A. Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis. Oncogene. 1999 Oct 21;18(43):5915-22. PMID:10557078 doi:http://dx.doi.org/10.1038/sj.onc.1202974
↑ Koshiba S, Kigawa T, Kikuchi A, Yokoyama S. Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin. J Struct Funct Genomics. 2002;2(1):1-8. PMID:12836669

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1inz"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN==
-<StructureSection load='1inz' size='340' side='right' caption='[[1inz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1inz' size='340' side='right'caption='[[1inz]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1inz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1INZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1inz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1INZ 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=1inz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inz OCA], [http://pdbe.org/1inz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1inz RCSB], [http://www.ebi.ac.uk/pdbsum/1inz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1inz ProSAT], [http://www.topsan.org/Proteins/RSGI/1inz TOPSAN]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1inz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inz OCA], [https://pdbe.org/1inz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1inz RCSB], [https://www.ebi.ac.uk/pdbsum/1inz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1inz ProSAT], [https://www.topsan.org/Proteins/RSGI/1inz TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/EPN1_HUMAN EPN1_HUMAN]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis.<ref>PMID:10557078</ref>
+[https://www.uniprot.org/uniprot/EPN1_HUMAN EPN1_HUMAN] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis.<ref>PMID:10557078</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/1inz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/1inz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1inz" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Epsin|Epsin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Kigawa, T]]
+[[Category: Homo sapiens]]
-[[Category: Kikuchi, A]]
+[[Category: Large Structures]]
-[[Category: Koshiba, S]]
+[[Category: Kigawa T]]
-[[Category: Structural genomic]]
+[[Category: Kikuchi A]]
-[[Category: Yokoyama, S]]
+[[Category: Koshiba S]]
-[[Category: Alpha-helix]]
+[[Category: Yokoyama S]]
-[[Category: Endocytosis-exocytosis complex]]
-[[Category: Epsin]]
-[[Category: Rsgi]]

1inz

From Proteopedia

Current revision

SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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