3c59: Difference between revisions

Revision as of 18:16, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3c59.png

3c59, resolution 2.30Å ()

Sites:

Ligands:

Non-Standard Residues:

Gene:

Glucagon-like peptide-1 receptor(GLP1R) (Homo sapiens)

Related:

3c5t

Structural annotation:
Resources:	UniProt : P43220, P26349

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domainCrystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain

Template:ABSTRACT PUBMED 18287102

About this StructureAbout this Structure

3C59 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal Structure of the Ligand-bound Glucagon-like Peptide-1 Receptor Extracellular Domain., Runge S, Thogersen H, Madsen K, Lau J, Rudolph R, J Biol Chem. 2008 Apr 25;283(17):11340-7. Epub 2008 Feb 20. PMID:18287102

Page seeded by OCA on Sun Jul 27 18:16:30 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain'''
+===Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain===
-==Overview==
+<!--
-The glucagon-like peptide-1 receptor (GLP-1R) belongs to Family B1 of the seven-transmembrane G protein-coupled receptors, and its natural agonist ligand is the peptide hormone glucagon-like peptide-1 (GLP-1). GLP-1 is involved in glucose homeostasis, and activation of GLP-1R in the plasma membrane of pancreatic beta-cells potentiates glucose-dependent insulin secretion. The N-terminal extracellular domain (nGLP-1R) is an important ligand binding domain that binds GLP-1 and the homologous peptide Exendin-4 with differential affinity. Exendin-4 has a C-terminal extension of nine amino acid residues known as the "Trp cage", which is absent in GLP-1. The Trp cage was believed to interact with nGLP-1R and thereby explain the superior affinity of Exendin-4. However, the molecular details that govern ligand binding and specificity of nGLP-1R remain undefined. Here we report the crystal structure of human nGLP-1R in complex with the antagonist Exendin-4(9-39) solved by the multiwavelength anomalous dispersion method to 2.2A resolution. The structure reveals that Exendin-4(9-39) is an amphipathic alpha-helix forming both hydrophobic and hydrophilic interactions with nGLP-1R. The Trp cage of Exendin-4 is not involved in binding to nGLP-1R. The hydrophobic binding site of nGLP-1R is defined by discontinuous segments including primarily a well defined alpha-helix in the N terminus of nGLP-1R and a loop between two antiparallel beta-strands. The structure provides for the first time detailed molecular insight into ligand binding of the human GLP-1 receptor, an established target for treatment of type 2 diabetes.
+The line below this paragraph, {{ABSTRACT_PUBMED_18287102}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18287102 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18287102}}
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