1by1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (23:22, 27 December 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1by1.png|left|200px]]
 
-
<!--
+
==DBL homology domain from beta-PIX==
-
The line below this paragraph, containing "STRUCTURE_1by1", creates the "Structure Box" on the page.
+
<StructureSection load='1by1' size='340' side='right'caption='[[1by1]]' 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'>[[1by1]] 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=1BY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY1 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">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=1by1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by1 OCA], [https://pdbe.org/1by1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by1 RCSB], [https://www.ebi.ac.uk/pdbsum/1by1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by1 ProSAT]</span></td></tr>
-
{{STRUCTURE_1by1| PDB=1by1 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ARHG7_HUMAN ARHG7_HUMAN] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.<ref>PMID:19041750</ref> <ref>PMID:18716323</ref> <ref>PMID:18184567</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/by/1by1_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=1by1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Guanine nucleotide exchange factors in the Dbl family activate Rho GTPases by accelerating dissociation of bound GDP, promoting acquisition of the GTP-bound state. Dbl proteins possess a approximately 200 residue catalytic Dbl-homology (DH) domain, that is arranged in tandem with a C-terminal pleckstrin homology (PH) domain in nearly all cases. Here we report the solution structure of the DH domain of human PAK-interacting exchange protein (betaPIX). The domain is composed of 11 alpha-helices that form a flattened, elongated bundle. The structure explains a large body of mutagenesis data, which, along with sequence comparisons, identify the GTPase interaction site as a surface formed by three conserved helices near the center of one face of the domain. Proximity of the site to the DH C-terminus suggests a means by which PH-ligand interactions may be coupled to DH-GTPase interactions to regulate signaling through the Dbl proteins in vivo.
-
===DBL homology domain from beta-PIX===
+
Structure and mutagenesis of the Dbl homology domain.,Aghazadeh B, Zhu K, Kubiseski TJ, Liu GA, Pawson T, Zheng Y, Rosen MK Nat Struct Biol. 1998 Dec;5(12):1098-107. PMID:9846881<ref>PMID:9846881</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1by1" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_9846881}}, adds the Publication Abstract to the page
+
*[[Rho guanine nucleotide exchange factor 3D structures|Rho guanine nucleotide exchange factor 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 9846881 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_9846881}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1BY1 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY1 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:9846881</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Aghazadeh, B.]]
+
[[Category: Large Structures]]
-
[[Category: Kubiseski, T J.]]
+
[[Category: Aghazadeh B]]
-
[[Category: Liu, G A.]]
+
[[Category: Kubiseski TJ]]
-
[[Category: Pawson, T.]]
+
[[Category: Liu GA]]
-
[[Category: Rosen, M K.]]
+
[[Category: Pawson T]]
-
[[Category: Zheng, Y.]]
+
[[Category: Rosen MK]]
-
[[Category: Zhu, K.]]
+
[[Category: Zheng Y]]
-
[[Category: Rho-gtpase exchange factor]]
+
[[Category: Zhu K]]
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:22:13 2009''
+

Current revision

DBL homology domain from beta-PIX

PDB ID 1by1

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/1by1"
Personal tools