3g9h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3g9h" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:3g9h.png|left|200px]]
+
==Crystal structure of the C-terminal mu homology domain of Syp1==
 +
<StructureSection load='3g9h' size='340' side='right' caption='[[3g9h]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3g9h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G9H FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g9g|3g9g]]</td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYP1, YCR030C, YCR30C/YCR29C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</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=3g9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g9h RCSB], [http://www.ebi.ac.uk/pdbsum/3g9h PDBsum]</span></td></tr>
 +
</table>
 +
== 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/g9/3g9h_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding mu homology domains (muHDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The muHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis.
-
{{STRUCTURE_3g9h| PDB=3g9h | SCENE= }}
+
Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.,Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B EMBO J. 2009 Oct 21;28(20):3103-16. Epub 2009 Aug 27. PMID:19713939<ref>PMID:19713939</ref>
-
===Crystal structure of the C-terminal mu homology domain of Syp1===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_19713939}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[3g9h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9H OCA].
+
</StructureSection>
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:019713939</ref><references group="xtra"/>
+
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Barker, S.]]
+
[[Category: Barker, S]]
-
[[Category: Hurley, J.]]
+
[[Category: Hurley, J]]
-
[[Category: Im, Y J.]]
+
[[Category: Im, Y J]]
-
[[Category: Maldonado-Baez, L.]]
+
[[Category: Maldonado-Baez, L]]
-
[[Category: Mishra, S.]]
+
[[Category: Mishra, S]]
-
[[Category: Reider, A.]]
+
[[Category: Reider, A]]
-
[[Category: Traub, L.]]
+
[[Category: Traub, L]]
-
[[Category: Wendland, B.]]
+
[[Category: Wendland, B]]
[[Category: Adaptor]]
[[Category: Adaptor]]
[[Category: Endocytosis]]
[[Category: Endocytosis]]

Revision as of 10:11, 3 December 2014

Crystal structure of the C-terminal mu homology domain of Syp1

3g9h, resolution 2.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3g9h"
Personal tools