Sandbox Reserved 429
From Proteopedia
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<scene name='Sandbox_Reserved_429/Whole/1'>BMP-7 Complex </scene> | <scene name='Sandbox_Reserved_429/Whole/1'>BMP-7 Complex </scene> | ||
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| + | BMP-7 uses two pairs of antiparallel β-strands referred as Finger 1 and Finger 2 for binding activities. The curvature of the fingers creates a site in which the α3 of the other subunit binds to stabilize the dimer. Free BMP-7 shows conformational changes in the "wrist" and "knuckles" areas upon complexing with receptors. | ||
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| + | Signaling by BMP-7 occurs by the binding of the protein to high affinity type II receptor (at the knuckle epitope) follow by the recruitment of the low affinity type I receptor (at the wrist epitope). The binding causes the trans-phosphorylation of the Type I receptor at a a glycine- and serine- rich region (GS-Box) by the type II receptor kinase. Afterwards the type I receptor Ser/Thr-kinase activates leading to intracellular signaling. | ||
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7. Overall Summary of how binding affects overall pathways for bone formation | 7. Overall Summary of how binding affects overall pathways for bone formation | ||
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===Additional Features=== | ===Additional Features=== | ||
Revision as of 20:08, 15 April 2012
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Contents |
YourMacromolecule
Introduction
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1. Basic info (size, ligand name)
2. Origin (Zebrafish?)
3. Relation to disease (Metastatic Prostate cancer, kidney disease)
4. Pharmaceutical Applications
Overall Structure
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1. Size of Protein
2. AA distribution
3. How many Domains
4. Number and locations of Alpha Helices, Beta Strands
5. Other pieces (non AA)
6. Primary Structure? Secondary? Tertiary?
Binding Interactions
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Draft
BMP-7 uses two pairs of antiparallel β-strands referred as Finger 1 and Finger 2 for binding activities. The curvature of the fingers creates a site in which the α3 of the other subunit binds to stabilize the dimer. Free BMP-7 shows conformational changes in the "wrist" and "knuckles" areas upon complexing with receptors.
Signaling by BMP-7 occurs by the binding of the protein to high affinity type II receptor (at the knuckle epitope) follow by the recruitment of the low affinity type I receptor (at the wrist epitope). The binding causes the trans-phosphorylation of the Type I receptor at a a glycine- and serine- rich region (GS-Box) by the type II receptor kinase. Afterwards the type I receptor Ser/Thr-kinase activates leading to intracellular signaling.
Outline
1. BMP7-Noggin Complex
2.Conformational changes due to binding
3. Hydrophilic and hydrophobic pockets
4. Receptor 1 & 2 and Finger 1 & 2
5. Others Antagonist of BMP 7
6. Binding affinity in comparison to others BMP families
7. Overall Summary of how binding affects overall pathways for bone formation
Additional Features
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1. Mutations in NOG
a.Substitutions of six positions :Pro35Arg, Cys184Tyr, Gly189Cys, Ile220Asn, Tyr222Cys/ Tyr222Asn, Pro223Leu affect folding stability
b. Pro35Arg - decreased affinity, diminished inhibition of chondrogenesis
c. Pro35Ser- similar
2. BMP regulators evolution -BMP signalling pathway, gene duplication ligand receptor - structural homology between agonists and antagonists
Credits
Introduction - Alec
Overall Structure - William
Drug Binding Site - Felix
Additional Features - Paula
