1ggn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:11, 9 August 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1ggn.png|left|200px]]
 
-
<!--
+
==Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design==
-
The line below this paragraph, containing "STRUCTURE_1ggn", creates the "Structure Box" on the page.
+
<StructureSection load='1ggn' size='340' side='right'caption='[[1ggn]], [[Resolution|resolution]] 2.36&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'>[[1ggn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GGN 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]] 2.36&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLS:BETA-D-GLUCOPYRANOSE+SPIROHYDANTOIN'>GLS</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-
{{STRUCTURE_1ggn| PDB=1ggn | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ggn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ggn OCA], [https://pdbe.org/1ggn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ggn RCSB], [https://www.ebi.ac.uk/pdbsum/1ggn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ggn ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
 +
== 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/gg/1ggn_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=1ggn ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Glucopyranosylidene spirothiohydantoin (TH) has been identified as a potential inhibitor of both muscle and liver glycogen phosphorylase b (GPb) and a (GPa) and shown to diminish liver GPa activity in vitro. Kinetic experiments reported here show that TH inhibits muscle GPb competitively with respect to both substrates phosphate (K(i)=2.3 microM) and glycogen (K(i)=2.8 microM). The structure of the GPb-TH complex has been determined at a resolution of 2.26 A and refined to a crystallographic R value of 0.193 (R(free)=0.211). The structure of GPb-TH complex reveals that the inhibitor can be accommodated in the catalytic site of T-state GPb with very little change of the tertiary structure, and provides a basis of understanding potency and specificity of the inhibitor. The glucopyranose moiety makes the standard hydrogen bonds and van der Waals contacts as observed in the glucose complex, while the rigid thiohydantoin group is in a favourable electrostatic environment and makes additional polar contacts to the protein.
-
===Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design===
+
Kinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase B.,Oikonomakos NG, Skamnaki VT, Osz E, Szilagyi L, Somsak L, Docsa T, Toth B, Gergely P Bioorg Med Chem. 2002 Feb;10(2):261-8. PMID:11741774<ref>PMID:11741774</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1ggn" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_11741774}}, adds the Publication Abstract to the page
+
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 11741774 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_11741774}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1GGN is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGN OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:11741774</ref><references group="xtra"/>
+
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Phosphorylase]]
+
[[Category: Fleet GW]]
-
[[Category: Fleet, G W.]]
+
[[Category: Gregoriou M]]
-
[[Category: Gregoriou, M.]]
+
[[Category: Johnson LN]]
-
[[Category: Johnson, L N.]]
+
[[Category: Oikonomakos NG]]
-
[[Category: Oikonomakos, N G.]]
+
[[Category: Skamnaki VT]]
-
[[Category: Skamnaki, V T.]]
+
[[Category: Tsitsanou KE]]
-
[[Category: Tsitsanou, K E.]]
+
[[Category: Watson KA]]
-
[[Category: Watson, K A.]]
+
[[Category: Zographos SE]]
-
[[Category: Zographos, S E.]]
+
-
[[Category: Catalytic site]]
+
-
[[Category: Design]]
+
-
[[Category: Glycogen phosphorylase]]
+
-
[[Category: Inhibitor complex]]
+
-
[[Category: Transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:31:46 2009''
+

Current revision

Structures of glycogen phosphorylase-inhibitor complexes and the implications for structure-based drug design

PDB ID 1ggn

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/1ggn"
Personal tools