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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Dergunov, Alexander D. |
| Description | Author Affiliation: Dergunov AD ( National Research Centre for Preventive Medicine, 10, Petroverigsky Street, 101990 Moscow, Russia. Electronic address: dergunov@img.ras.ru.) |
| Abstract | Twenty-nine from 52 missense mutations in apoA-I gene are predicted to be deleterious by both SIFT and PolyPhen-2 algorithms. Among those, eight mutations with a prominent change in structure stability as modeled by the SDM tool for both lipid-free (Mei and Atkinson (2011) PDB ID: 3R2P ) and HDL-bound (Wu et al. (2009) PDB ID: 3K2S ) apoA-I, are referred as structural. The remaining mutations with a preferential location in a long intrinsically disordered region, predicted by the SPINE-D and DNdisorder tools, may influence the functional sites. Among structural mutations, five amyloidosis-only-related mutations, significant in a lipid-free structure, are located in 1–90 region. Six amyloidosis- and hypoalphalipoproteinemia-associated mutations, differently significant in two chains of lipid-bound apoA-I, are distributed among the N-domain. Six cholesterol recognition putative motifs (5 CRAC/1 CCM) in apoA-I structure are suggested to interact with cholesterol. Among those, the K40-W50 partially conserved CCM sequence with a putative recognition feature, predicted by the MoRF tool, may underlie cholesterol binding to lipid-free apoA-I, the binding triggering the disorder-to-order transition within MoRF. Thus, the impairment of helix formation and accelerated protein aggregation may underlie the amyloidogenic effect of W50R substitution. Also, D102H substitution in conserved CRAC2 V97-K106 sequence may be harmful in reverse cholesterol transport. With PDBe Motifs and Sites algorithm, cholesterol is a ligand for L101, F104 and W108 residues in HDL-bound apoA-I. The influence of specific mutation on apoA-I structure and mutated apolipoprotein switch between different pathologies is suggested to depend on the surrounding phase properties. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 10 |
| Volume Number | 1834 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-10-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Apolipoprotein A-I Genetics Cholesterol Chemistry Lipoproteins, HDL Mutation, Missense Polymorphism, Single Nucleotide Algorithms Amino Acid Sequence Amino Acid Substitution Amyloidosis Metabolism Pathology Binding Sites Circular Dichroism Hypoalphalipoproteinemias Molecular Sequence Data Protein Binding Protein Interaction Domains And Motifs Protein Structure, Secondary Sequence Alignment Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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