3qmk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:48, 21 February 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3qmk.png|left|200px]]
 
-
<!--
+
==Crystal structure of the E2 domain of APLP1 in complex with heparin hexasaccharide==
-
The line below this paragraph, containing "STRUCTURE_3qmk", creates the "Structure Box" on the page.
+
<StructureSection load='3qmk' size='340' side='right'caption='[[3qmk]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3qmk]] is a 2 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=3QMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QMK FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_3qmk| PDB=3qmk | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qmk OCA], [https://pdbe.org/3qmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qmk RCSB], [https://www.ebi.ac.uk/pdbsum/3qmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qmk ProSAT]</span></td></tr>
-
 
+
</table>
-
===Crystal structure of the E2 domain of APLP1 in complex with heparin hexasaccharide===
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/APLP1_HUMAN APLP1_HUMAN] May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I. The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis.
-
 
+
__TOC__
-
<!--
+
</StructureSection>
-
The line below this paragraph, {{ABSTRACT_PUBMED_21930949}}, adds the Publication Abstract to the page
+
-
(as it appears on PubMed at http://www.pubmed.gov), where 21930949 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_21930949}}
+
-
 
+
-
==About this Structure==
+
-
[[3qmk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QMK OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:021930949</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Ha, Y.]]
+
[[Category: Large Structures]]
-
[[Category: Xue, Y.]]
+
[[Category: Ha Y]]
-
[[Category: Alzheimer's disease]]
+
[[Category: Xue Y]]
-
[[Category: App]]
+
-
[[Category: Brain]]
+
-
[[Category: Cell adhesion]]
+
-
[[Category: Cellular adhesion]]
+
-
[[Category: Heparin]]
+

Current revision

Crystal structure of the E2 domain of APLP1 in complex with heparin hexasaccharide

PDB ID 3qmk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools