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2qll

From Proteopedia

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Revision as of 10:51, 5 September 2018

Human liver glycogen phosphorylase- GL complex

Structural highlights

2qll is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1fa9, 1fc0
Gene:	PYGL (HUMAN)
Activity:	Phosphorylase, with EC number 2.4.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[PYGL_HUMAN] Defects in PYGL are the cause of glycogen storage disease type 6 (GSD6) [MIM:232700]. A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected.^[1]

Function

[PYGL_HUMAN] 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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Disrupting the interaction between glycogen phosphorylase and the glycogen targeting subunit (G(L)) of protein phosphatase 1 is emerging as a novel target for the treatment of type 2 diabetes. To elucidate the molecular basis of binding, we have determined the crystal structure of liver phosphorylase bound to a G(L)-derived peptide. The structure reveals the C terminus of G(L) binding in a hydrophobically collapsed conformation to the allosteric regulator-binding site at the phosphorylase dimer interface. G(L) mimics interactions that are otherwise employed by the activator AMP. Functional studies show that G(L) binds tighter than AMP and confirm that the C-terminal Tyr-Tyr motif is the major determinant for G(L) binding potency. Our study validates the G(L)-phosphorylase interface as a novel target for small molecule interaction.

Molecular recognition of the protein phosphatase 1 glycogen targeting subunit by glycogen phosphorylase.,Pautsch A, Stadler N, Wissdorf O, Langkopf E, Moreth W, Streicher R J Biol Chem. 2008 Apr 4;283(14):8913-8. Epub 2008 Jan 15. PMID:18198182^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Burwinkel B, Bakker HD, Herschkovitz E, Moses SW, Shin YS, Kilimann MW. Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Am J Hum Genet. 1998 Apr;62(4):785-91. PMID:9529348
↑ Pautsch A, Stadler N, Wissdorf O, Langkopf E, Moreth W, Streicher R. Molecular recognition of the protein phosphatase 1 glycogen targeting subunit by glycogen phosphorylase. J Biol Chem. 2008 Apr 4;283(14):8913-8. Epub 2008 Jan 15. PMID:18198182 doi:10.1074/jbc.M706612200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qll"

@@ Line 1: / Line 1: @@
 ==Human liver glycogen phosphorylase- GL complex==
 <StructureSection load='2qll' size='340' side='right' caption='[[2qll]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
@@ Line 8: / Line 9: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYGL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qll OCA], [http://pdbe.org/2qll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qll RCSB], [http://www.ebi.ac.uk/pdbsum/2qll PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qll OCA], [http://pdbe.org/2qll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qll RCSB], [http://www.ebi.ac.uk/pdbsum/2qll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qll ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 18: / Line 19: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ql/2qll_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ql/2qll_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2qll

From Proteopedia

Revision as of 10:51, 5 September 2018

Human liver glycogen phosphorylase- GL complex

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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