Dynamic interaction among the platform domain and two membrane-proximal immunoglobulin-like domains of class I major histocompatibility complex: normal mode analysis.
作者： Hiroyuki Nojima , Mayuko Takeda-Shitaka , Kazuhiko Kanou , Kenshu Kamiya , Hideaki Umeyama
DOI: 10.1248/CPB.56.635
关键词:
摘要: Class I major histocompatibility complex (MHC) molecules have three domains, a platform domain and two membrane-proximal immunoglobulin-like an α3 β2-immunoglobulin (β2m). To understand the dynamic interactions among we simulated behavior of partial model deficient in β2m another domain, by normal mode analysis. As result, was more flexible interdomain conformation than other model. The lowest frequency modes (<2 cm−1) observed for simulations showed clear motions as if each moved like rigid body. Such low frequencies were not model, therefore flexibility may be due to cm−1). These results suggest that contributes maintaining class MHC does, offer convincing evidence support notion do equal influence on structural stability molecules.
sci-hub.se 参考文章(38)
Hisashi Ishida, Yasumasa Jochi, Akinori Kidera, Dynamic structure of subtilisin-eglin c complex studied by normal mode analysis Proteins: Structure, Function, and Genetics. ,vol. 32, pp. 324- 333 ,(1998) , 10.1002/(SICI)1097-0134(19980815)32:3<324::AID-PROT8>3.0.CO;2-H
K. L. Rock, L. E. Rothstein, S. R. Gamble, B. Benacerraf, Reassociation with beta 2-microglobulin is necessary for Kb class I major histocompatibility complex binding of exogenous peptides. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 87, pp. 7517- 7521 ,(1990) , 10.1073/PNAS.87.19.7517
Hiroyuki Nojima, Mayuko Takeda-Shitaka, Youji Kurihara, Kenshu Kamiya, Hideaki Umeyama, Dynamic Flexibility of a Peptide-Binding Groove of Human HLA-DR1 Class II MHC Molecules: Normal Mode Analysis of the Antigen Peptide–Class II MHC Complex CHEMICAL & PHARMACEUTICAL BULLETIN. ,vol. 51, pp. 923- 928 ,(2003) , 10.1248/CPB.51.923
Hiroshi Wako, Dynamic structures of globular proteins with respect to correlative movements of residues calculated in the normal mode analysis Journal of Protein Chemistry. ,vol. 8, pp. 589- 607 ,(1989) , 10.1007/BF01025600
Scott J. Weiner, Peter A. Kollman, David A. Case, U. Chandra Singh, Caterina Ghio, Guliano Alagona, Salvatore Profeta, Paul Weiner, A NEW FORCE FIELD FOR MOLECULAR MECHANICAL SIMULATION OF NUCLEIC ACIDS AND PROTEINS Journal of the American Chemical Society. ,vol. 106, pp. 765- 784 ,(1984) , 10.1021/JA00315A051
Kevin P. Kane, Linda A. Sherman, Matthew F. Mescher, Exogenous β2‐microglobulin is required for antigenic peptide binding to isolated class I major histocompatibility complex molecules European Journal of Immunology. ,vol. 21, pp. 2289- 2292 ,(1991) , 10.1002/EJI.1830210945
Hiromi SUMIKAWA, Ei-ichiro SUZUKI, Ken-ichi FUKUHARA, Yasushi NAKAJIMA, Kenshu KAMIYA, Hideaki UMEYAMA, Dynamic structures of granulocyte colony-stimulating factor proteins studied by normal mode analysis: Two domain-type motions in low frequency modes Chemical & Pharmaceutical Bulletin. ,vol. 46, pp. 1069- 1077 ,(1998) , 10.1248/CPB.46.1069
A Vitiello, T. Potter, L. Sherman, The role of beta 2-microglobulin in peptide binding by class I molecules Science. ,vol. 250, pp. 1423- 1426 ,(1990) , 10.1126/SCIENCE.2124002
N. Go, T. Noguti, T. Nishikawa, Dynamics of a small globular protein in terms of low-frequency vibrational modes Proceedings of the National Academy of Sciences of the United States of America. ,vol. 80, pp. 3696- 3700 ,(1983) , 10.1073/PNAS.80.12.3696
K. L. Rock, S. Gamble, L. Rothstein, B. Benacerraf, Reassociation with beta 2-microglobulin is necessary for Db class I major histocompatibility complex binding of an exogenous influenza peptide Proceedings of the National Academy of Sciences of the United States of America. ,vol. 88, pp. 301- 304 ,(1991) , 10.1073/PNAS.88.1.301