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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Feng, Ye-dan Li, Jing Zhou, Wen-chang Jia, Zhi-guang Wei, Qun |
| Description | Author Affiliation: Feng YD ( Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing, People's Republic of China.) |
| Abstract | EF-hand calcium binding proteins (CaBPs) share strong sequence homology, but exhibit great diversity in structure and function. Thus although calmodulin (CaM) and calcineurin B (CNB) both consist of four EF hands, their domain arrangements are quite distinct. CaM and the CaM-like proteins are characterized by an extended architecture, whereas CNB and the CNB-like proteins have a more compact form. In this study, we performed structural alignments and molecular dynamics (MD) simulations on 3 CaM-like proteins and 6 CNB-like proteins, and quantified their distinct structural and dynamical features in an effort to establish how their sequences specify their structures and dynamics. Alignments of the EF2–EF3 region of these proteins revealed that several residues (not restricted to the linker between the EF2 and EF3 motifs) differed between the two groups of proteins. A customized inverse folding approach followed by structural assessments and MD simulations established the critical role of these residues in determining the structure of the proteins. Identification of the critical determinants of the two different EF-hand domain arrangements and the distinct dynamical features relevant to their respective functions provides insight into the relationships between sequence, structure, dynamics and function among these EF-hand CaBPs. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1824 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Calcineurin Chemistry Calmodulin Molecular Dynamics Simulation Amino Acid Motifs Amino Acid Sequence Animals Molecular Sequence Data Phylogeny Protein Stability Protein Structure, Tertiary Rabbits Sequence Homology, Amino Acid Structural Homology, Protein Comparative Study Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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