2iug

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:29, 9 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_2iug| PDB=2iug | SCENE= }}
 
-
===CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN===
 
-
{{ABSTRACT_PUBMED_8599763}}
 
-
==About this Structure==
+
==Crystal structure of the PI3-kinase p85 N-terminal SH2 domain==
-
[[2iug]] is a 1 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=2IUG OCA].
+
<StructureSection load='2iug' size='340' side='right'caption='[[2iug]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2iug]] 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=2IUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUG FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</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=2iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iug OCA], [https://pdbe.org/2iug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iug RCSB], [https://www.ebi.ac.uk/pdbsum/2iug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iug ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/P85A_HUMAN P85A_HUMAN] Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling.<ref>PMID:7518429</ref> <ref>PMID:17626883</ref> <ref>PMID:19805105</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/iu/2iug_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/main_output.php?pdb_ID=2iug ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Crystal structures of the amino-terminal SH2 domain of the p85alpha subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphopeptides bind in the two-pronged manner seen in high-affinity Lck and Src SH2 complexes, with conserved interactions between the domain and the peptide segment from phosphotyrosine to Met+3. Peptide binding requires the rearrangement of a tyrosyl side chain in the BG loop to create the hydrophobic Met+3 binding pocket. The structures suggest a mechanism for the biological specificity exhibited by PI 3-kinase in its interactions with phosphoprotein partners.
-
==See Also==
+
Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes.,Nolte RT, Eck MJ, Schlessinger J, Shoelson SE, Harrison SC Nat Struct Biol. 1996 Apr;3(4):364-74. PMID:8599763<ref>PMID:8599763</ref>
-
*[[Phosphoinositide 3-Kinases|Phosphoinositide 3-Kinases]]
+
-
*[[Phsphatidylinositol 3-kinase|Phsphatidylinositol 3-kinase]]
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:008599763</ref><references group="xtra"/>
+
</div>
 +
<div class="pdbe-citations 2iug" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Phosphoinositide 3-kinase 3D structures|Phosphoinositide 3-kinase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Eck, M J.]]
+
[[Category: Large Structures]]
-
[[Category: Harrison, S C.]]
+
[[Category: Eck MJ]]
-
[[Category: Nolte, R T.]]
+
[[Category: Harrison SC]]
-
[[Category: Schlessinger, J.]]
+
[[Category: Nolte RT]]
-
[[Category: Shoelson, S E.]]
+
[[Category: Schlessinger J]]
-
[[Category: Disease mutation]]
+
[[Category: Shoelson SE]]
-
[[Category: P85]]
+
-
[[Category: Phosphorylation]]
+
-
[[Category: Pi3-kinase]]
+
-
[[Category: Pi3k]]
+
-
[[Category: Sh2]]
+
-
[[Category: Sh2 domain]]
+
-
[[Category: Sh3 domain]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of the PI3-kinase p85 N-terminal SH2 domain

PDB ID 2iug

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/2iug"
Personal tools