INT81788

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Context Info
Confidence 0.51
First Reported 1999
Last Reported 2003
Negated 0
Speculated 0
Reported most in Abstract
Documents 4
Total Number 10
Disease Relevance 0
Pain Relevance 1.09

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extracellular space (AGRP) extracellular region (AGRP) Golgi apparatus (AGRP)
plasma membrane (MC4R) signal transducer activity (MC4R)
AGRP (Homo sapiens)
MC4R (Homo sapiens)
Pain Link Frequency Relevance Heat
antagonist 10 98.04 Very High Very High Very High
melanocortin 1 receptor 10 97.92 Very High Very High Very High

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Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
However, the detailed molecular basis of MC4R domains in AGRP binding is presently unclear.
AGRP Binding (binding) of MC4R
1) Confidence 0.51 Published 2003 Journal Mol. Pharmacol. Section Abstract Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.13
Our previous studies have suggested that in addition to exoloops 2 and 3, several transmembrane domains of MC4R may be important for AGRP binding.
AGRP Binding (binding) of MC4R
2) Confidence 0.51 Published 2003 Journal Mol. Pharmacol. Section Abstract Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.12
The present studies were designed to examine the contribution of extracytoplasmic domains of the melanocortin-4 receptor (MC4R) to AGRP binding by making chimerical receptor constructs of the human melanocortin-1 receptor (MC1R; a receptor that is not inhibited by AGRP) and the human MC4R (a receptor that is potently inhibited by AGRP).
AGRP Binding (binding) of MC4R associated with melanocortin 1 receptor
3) Confidence 0.40 Published 1999 Journal J. Biol. Chem. Section Abstract Doc Link 10318826 Disease Relevance 0 Pain Relevance 0.14
The present studies were designed to examine the contribution of extracytoplasmic domains of the melanocortin-4 receptor (MC4R) to AGRP binding by making chimerical receptor constructs of the human melanocortin-1 receptor (MC1R; a receptor that is not inhibited by AGRP) and the human MC4R (a receptor that is potently inhibited by AGRP).
AGRP Binding (binding) of melanocortin-4 receptor associated with melanocortin 1 receptor
4) Confidence 0.40 Published 1999 Journal J. Biol. Chem. Section Abstract Doc Link 10318826 Disease Relevance 0 Pain Relevance 0.14
The present studies were designed to determine the specific contribution of MC4R exoloops and transmembrane domains to AGRP binding by using chimeric receptor constructs of the human melanocortin-1 receptor (hMC1R), a receptor that is not inhibited by AGRP, and the human MC4R (hMC4R), a receptor that is potently inhibited by AGRP.
AGRP Binding (binding) of MC4R associated with melanocortin 1 receptor
5) Confidence 0.40 Published 2003 Journal Mol. Pharmacol. Section Abstract Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.14
Conversely, the exchange of exoloops 2 and 3 of the MC1R with the homologous exoloops of the MC4R was found to confer AGRP binding and inhibitory activity to the basic structure of the MC1R.
AGRP Binding (binding) of MC4R
6) Confidence 0.35 Published 1999 Journal J. Biol. Chem. Section Abstract Doc Link 10318826 Disease Relevance 0 Pain Relevance 0.10
The second and third extracellular loops of MC4R are important for AGRP 87-132 N-terminal binding, whereas the third and fourth transmembrane domains of hMC4R are crucial for AGRP 110-117 binding.
AGRP Binding (binding) of MC4R
7) Confidence 0.33 Published 2003 Journal Mol. Pharmacol. Section Abstract Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.07
Molecular determination of agouti-related protein binding to human melanocortin-4 receptor.
agouti-related protein Binding (binding) of melanocortin-4 receptor
8) Confidence 0.33 Published 2003 Journal Mol. Pharmacol. Section Title Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.13
These data suggest that the AGRP fragment 110-117 has no binding sites at exoloops of hMC4R and that transmembrane domains of MC4R may play an important role in AGRP 110-117 binding and function, whereas the exoloops do not.
AGRP Binding (binding) of MC4R
9) Confidence 0.33 Published 2003 Journal Mol. Pharmacol. Section Abstract Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.07
The second and third extracellular loops of MC4R are important for AGRP 87-132 N-terminal binding, whereas the third and fourth transmembrane domains of hMC4R are crucial for AGRP 110-117 binding.
AGRP Binding (binding) of hMC4R
10) Confidence 0.29 Published 2003 Journal Mol. Pharmacol. Section Abstract Doc Link 12815165 Disease Relevance 0 Pain Relevance 0.06

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