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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cho, Hyun-soo Kim, Minsup Yun, Ji-hye Ko, Yoon-joo Jung, Youngjin Cho, Art E. Lee, Weontae Kim, Kuglae Lee, Dongju Oh, Daeseok |
| Description | Author Affiliation: Yun JH ( Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.); Kim M ( Department of Bioinformatics, Korea University, Sejong 136-701, Republic of Korea.); Kim K ( Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.); Lee D ( Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.); Jung Y ( Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.); Oh D ( Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.); Ko YJ ( National Center for Inter-University Research Facilities, Seoul National University, Seoul 151-747, Republic of Korea.); Cho AE ( Department of Bioinformatics, Korea University, Sejong 136-701, Republic of Korea.); Cho HS ( Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea.); Lee W ( Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Republic of Korea. Electronic address: wlee@spin.yonsei.ac.kr.) |
| Abstract | The melanocortin receptors (MCRs) are members of the G protein-coupled receptor (GPCR) 1 superfamily with seven transmembrane (TM) domains. Among them, the melanocortin-4 receptor (MC4R) subtype has been highlighted recently by genetic studies in obese humans. In particular, in a patient with severe early-onset obesity, a novel heterozygous mutation in the MC4R gene was found in an exchange of Asp to Asn in the 90th amino acid residue located in the TM 2 domain (MC4R $^{D90N}$ ). Mutations in the MC4R gene are the most frequent monogenic causes of severe obesity and are described as heterozygous with loss of function. We determine solution structures of the TM 2 domain of MC4R (MC4R $^{TM2}$ ) and compared secondary structure of Asp90 mutant (MC4R $^{TM2-D90N}$ ) in a micelle environment by nuclear magnetic resonance (NMR) spectroscopy. NMR structure shows that MC4R $^{TM2}$ forms a long α-helix with a kink at Gly98. Interestingly, the structure of MC4R $^{TM2-D90N}$ is similar to that of MC4R $^{TM2}$ based on data from CD and NMR spectrum. However, the thermal stability and homogeneity of MC4R $^{D90N}$ is quite different from those of MC4R. The structure from molecular modeling suggests that Asp90 $^{2.50}$ plays a key role in allosteric sodium ion binding. Our data suggest that the sodium ion interaction of Asp90 $^{2.50}$ in the allosteric pocket of MC4R is essential to its function, explaining the loss of function of the MC4R $^{D90N}$ mutant. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 6 |
| Volume Number | 1848 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-06-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Mutant Proteins Chemistry Metabolism Receptor, Melanocortin, Type 4 Sodium Dodecyl Sulfate Amino Acid Sequence Binding Sites Circular Dichroism Ions Magnetic Resonance Spectroscopy Micelles Models, Molecular Molecular Sequence Data Protein Stability Protein Structure, Secondary Isolation & Purification Pharmacology Sodium Structural Homology, Protein Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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