1z6p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (22:19, 26 March 2025) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1z6p.jpg|left|200px]]
 
-
{{Structure
+
==Glycogen phosphorylase AMP site inhibitor complex==
-
|PDB= 1z6p |SIZE=350|CAPTION= <scene name='initialview01'>1z6p</scene>, resolution 2.40&Aring;
+
<StructureSection load='1z6p' size='340' side='right'caption='[[1z6p]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=194:4-{2-[(3-NITROBENZOYL)AMINO]PHENOXY}PHTHALIC ACID'>194</scene>
+
<table><tr><td colspan='2'>[[1z6p]] 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=1Z6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z6P FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=194:4-{2-[(3-NITROBENZOYL)AMINO]PHENOXY}PHTHALIC+ACID'>194</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=1z6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z6p OCA], [https://pdbe.org/1z6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z6p RCSB], [https://www.ebi.ac.uk/pdbsum/1z6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z6p 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/z6/1z6p_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1z6p ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Inhibition of glycogen phosphorylase (GP) has attracted considerable attention during the last five to 10 years as a means of treating the elevated hepatic glucose production seen in patients with type 2 diabetes. Several different GP inhibitors binding to various binding sites of the GP enzyme have been reported in the literature. In this paper we report on a novel class of compounds that have been identified as potent GP inhibitors. Their synthesis, mode of binding to the allosteric AMP site as well as in vitro data on GP inhibition are shown. The most potent inhibitor was found to be 4-[2,4-bis-(3-nitrobenzoylamino)phenoxy]phthalic acid (4j) with an IC(50) value of 74 nM. This compound together with a closely related analogue was further characterized by enzyme kinetics and in primary rat hepatocytes.
-
'''Glycogen phosphorylase AMP site inhibitor complex'''
+
Identification, synthesis, and characterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site.,Kristiansen M, Andersen B, Iversen LF, Westergaard N J Med Chem. 2004 Jul 1;47(14):3537-45. PMID:15214781<ref>PMID:15214781</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1z6p" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Inhibition of glycogen phosphorylase (GP) has attracted considerable attention during the last five to 10 years as a means of treating the elevated hepatic glucose production seen in patients with type 2 diabetes. Several different GP inhibitors binding to various binding sites of the GP enzyme have been reported in the literature. In this paper we report on a novel class of compounds that have been identified as potent GP inhibitors. Their synthesis, mode of binding to the allosteric AMP site as well as in vitro data on GP inhibition are shown. The most potent inhibitor was found to be 4-[2,4-bis-(3-nitrobenzoylamino)phenoxy]phthalic acid (4j) with an IC(50) value of 74 nM. This compound together with a closely related analogue was further characterized by enzyme kinetics and in primary rat hepatocytes.
+
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1Z6P is a [[Single protein]] 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=1Z6P OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
Identification, synthesis, and characterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site., Kristiansen M, Andersen B, Iversen LF, Westergaard N, J Med Chem. 2004 Jul 1;47(14):3537-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15214781 15214781]
+
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Phosphorylase]]
+
[[Category: Andersen B]]
-
[[Category: Single protein]]
+
[[Category: Iversen LF]]
-
[[Category: Andersen, B.]]
+
[[Category: Kristiansen M]]
-
[[Category: Iversen, L F.]]
+
[[Category: Westergaard N]]
-
[[Category: Kristiansen, M.]]
+
-
[[Category: Westergaard, N.]]
+
-
[[Category: 194]]
+
-
[[Category: glycogen metabolism; glycogen phosphorylase b; inhibition; allosteric]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:31:49 2008''
+

Current revision

Glycogen phosphorylase AMP site inhibitor complex

PDB ID 1z6p

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/1z6p"
Personal tools