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- PDB-1y7k: NMR structure family of Human Agouti Signalling Protein (80-132: ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1y7k | ||||||
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Title | NMR structure family of Human Agouti Signalling Protein (80-132: Q115Y, S124Y) | ||||||
![]() | Agouti Signaling Protein | ||||||
![]() | SIGNALING PROTEIN / Melanocortin / inhibitor / cystine knot / GPCR / endogenous antagonist / inverse agonist | ||||||
Function / homology | ![]() melanocortin receptor binding / type 3 melanocortin receptor binding / type 4 melanocortin receptor binding / adult feeding behavior / melanosome transport / positive regulation of melanin biosynthetic process / melanin biosynthetic process / melanosome organization / epigenetic programming in the zygotic pronuclei / neuropeptide hormone activity ...melanocortin receptor binding / type 3 melanocortin receptor binding / type 4 melanocortin receptor binding / adult feeding behavior / melanosome transport / positive regulation of melanin biosynthetic process / melanin biosynthetic process / melanosome organization / epigenetic programming in the zygotic pronuclei / neuropeptide hormone activity / hormone-mediated signaling pathway / generation of precursor metabolites and energy / cell-cell signaling / signaling receptor binding / signal transduction / extracellular space Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Model type details | minimized average | ||||||
![]() | McNulty, J.C. / Jackson, P.J. / Thompson, D.A. / Chai, B. / Gantz, I. / Barsh, G.S. / Dawson, P.E. / Millhauser, G.L. | ||||||
![]() | ![]() Title: Structures of the agouti signaling protein. Authors: McNulty, J.C. / Jackson, P.J. / Thompson, D.A. / Chai, B. / Gantz, I. / Barsh, G.S. / Dawson, P.E. / Millhauser, G.L. #1: ![]() Title: High-resolution NMR structure of the chemically-synthesized melanocortin receptor binding domain AGRP(87-132) of the agouti-related protein Authors: McNulty, J.C. / Thompson, D.A. / Bolin, K.A. / Wilken, J. / Barsh, G.S. / Millhauser, G.L. #2: ![]() Title: Design, pharmacology, and NMR structure of a minimized cystine knot with agouti-related protein activity Authors: Jackson, P.J. / McNulty, J.C. / Yang, Y.K. / Thompson, D.A. / Chai, B. / Gantz, I. / Barsh, G.S. / Millhauser, G.L. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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-Validation report
Summary document | ![]() | 359.6 KB | Display | ![]() |
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Full document | ![]() | 505.9 KB | Display | |
Data in XML | ![]() | 16 KB | Display | |
Data in CIF | ![]() | 24.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 5823.997 Da / Num. of mol.: 1 / Fragment: residies 80-132 / Mutation: Q115Y, S124Y / Source method: obtained synthetically Details: Sequence occurs naturally in humans, genes ASIP, AGTI, AGTIL, ASP References: UniProt: P42127 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques, in conjunction with a semi-automated assignment protocol. |
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Sample preparation
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Sample conditions |
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-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 Details: This structure family represents one of two major conformers present in solution. The two conformers arise from the cis-trans proline isomerization of the Ala104-Pro105 peptide bond. | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 1000 / Conformers submitted total number: 21 Distance constraint violation method: From the original family of twenty, the representative conformer had the lowest target function and was subjected to further minimization in water. The remaining ...Distance constraint violation method: From the original family of twenty, the representative conformer had the lowest target function and was subjected to further minimization in water. The remaining structures were obtained without explicit inclusion of solvent. |