1dg3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:24, 22 May 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1dg3.png|left|200px]]
 
-
<!--
+
==STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM==
-
The line below this paragraph, containing "STRUCTURE_1dg3", creates the "Structure Box" on the page.
+
<StructureSection load='1dg3' size='340' side='right'caption='[[1dg3]], [[Resolution|resolution]] 1.80&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'>[[1dg3]] 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=1DG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DG3 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]] 1.8&#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=1dg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg3 OCA], [https://pdbe.org/1dg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dg3 ProSAT]</span></td></tr>
-
{{STRUCTURE_1dg3| PDB=1dg3 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GBP1_HUMAN GBP1_HUMAN] Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.<ref>PMID:22106366</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/dg/1dg3_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=1dg3 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Interferon-gamma is an immunomodulatory substance that induces the expression of many genes to orchestrate a cellular response and establish the antiviral state of the cell. Among the most abundant antiviral proteins induced by interferon-gamma are guanylate-binding proteins such as GBP1 and GBP2. These are large GTP-binding proteins of relative molecular mass 67,000 with a high-turnover GTPase activity and an antiviral effect. Here we have determined the crystal structure of full-length human GBP1 to 1.8 A resolution. The amino-terminal 278 residues constitute a modified G domain with a number of insertions compared to the canonical Ras structure, and the carboxy-terminal part is an extended helical domain with unique features. From the structure and biochemical experiments reported here, GBP1 appears to belong to the group of large GTP-binding proteins that includes Mx and dynamin, the common property of which is the ability to undergo oligomerization with a high concentration-dependent GTPase activity.
-
===STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM===
+
Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins.,Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C Nature. 2000 Feb 3;403(6769):567-71. PMID:10676968<ref>PMID:10676968</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_10676968}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1dg3" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 10676968 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_10676968}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1DG3 is a 1 chain structure of 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=1DG3 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:10676968</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Herrmann, C.]]
+
[[Category: Large Structures]]
-
[[Category: Praefcke, G J.K.]]
+
[[Category: Herrmann C]]
-
[[Category: Prakash, B.]]
+
[[Category: Praefcke GJK]]
-
[[Category: Renault, L.]]
+
[[Category: Prakash B]]
-
[[Category: Wittinghofer, A.]]
+
[[Category: Renault L]]
-
[[Category: Dynamin related]]
+
[[Category: Wittinghofer A]]
-
[[Category: Gbp]]
+
-
[[Category: Gdp]]
+
-
[[Category: Gmp]]
+
-
[[Category: Gtp hydrolysis]]
+
-
[[Category: Interferon induced]]
+
-
[[Category: Large gtpase family]]
+
-
[[Category: Signaling protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:42:58 2009''
+

Current revision

STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM

PDB ID 1dg3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools