4d5m

Gonadotropin-releasing hormone agonist

spinqualitylabelsall models 4d5m, resolution 0.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d5m is a 4 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.85Å Ligands: DTR, NH2, PCA, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease GON1_HUMAN Normosmic congenital hypogonadotropic hypogonadism. The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. The genetics of hypogonadotropic hypogonadism involves various modes of transmission. Oligogenic inheritance has been reported in some patients carrying mutations in GNRH1 as well as in other HH-associated genes including PROKR2 and FGFR1 (PubMed:23643382). Function GON1_HUMAN Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. Publication Abstract from PubMed External stimuli are powerful tools that naturally control protein assemblies and functions. For example, during viral entry and exit changes in pH are known to trigger large protein conformational changes. However, the molecular features stabilizing the higher pH structures remain unclear. Here we elucidate the conformational change of a self-assembling peptide that forms either small or large nanotubes dependent on the pH. The sub-angstrom high-pH peptide structure reveals a globular conformation stabilized through a strong histidine-serine H-bond and a tight histidine-aromatic packing. Lowering the pH induces histidine protonation, disrupts these interactions and triggers a large change to an extended beta-sheet-based conformation. Re-visiting available structures of proteins with pH-dependent conformations reveals both histidine-containing aromatic pockets and histidine-serine proximity as key motifs in higher pH structures. The mechanism discovered in this study may thus be generally used by pH-dependent proteins and opens new prospects in the field of nanomaterials. Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins.,Valery C, Deville-Foillard S, Lefebvre C, Taberner N, Legrand P, Meneau F, Meriadec C, Delvaux C, Bizien T, Kasotakis E, Lopez-Iglesias C, Gall A, Bressanelli S, Le Du MH, Paternostre M, Artzner F Nat Commun. 2015 Jul 20;6:7771. doi: 10.1038/ncomms8771. PMID:26190377 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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