6a9y: Difference between revisions

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==The crystal structure of Mu homology domain of SGIP1==
==The crystal structure of Mu homology domain of SGIP1==
<StructureSection load='6a9y' size='340' side='right' caption='[[6a9y]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='6a9y' size='340' side='right'caption='[[6a9y]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6a9y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A9Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[6a9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A9Y FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGIP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=6a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9y OCA], [http://pdbe.org/6a9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9y RCSB], [http://www.ebi.ac.uk/pdbsum/6a9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9y ProSAT]</span></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=6a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9y OCA], [https://pdbe.org/6a9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a9y RCSB], [https://www.ebi.ac.uk/pdbsum/6a9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SGIP1_HUMAN SGIP1_HUMAN]] May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis (By similarity).  
[https://www.uniprot.org/uniprot/SGIP1_HUMAN SGIP1_HUMAN] May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Feng, Y]]
[[Category: Large Structures]]
[[Category: Liu, X]]
[[Category: Feng Y]]
[[Category: Dimer]]
[[Category: Liu X]]
[[Category: Disulfide bond]]
[[Category: Endocytosis]]
[[Category: Sgip1]]

Latest revision as of 09:21, 22 November 2023

The crystal structure of Mu homology domain of SGIP1

6a9y, resolution 2.70Å

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