AI Article Synopsis
- - The 37/67-kDa human laminin receptor (LamR) is a protein on cell surfaces that plays a crucial role in cell adhesion and various biological processes by interacting with extracellular matrix molecules, especially laminins.
- - The specific way that laminin-1 binds to LamR is still not completely understood, but it's believed to involve regions of the protein called peptide G and the C-terminal helix.
- - Recent molecular dynamics simulations reveal that a flexible loop in LamR undergoes a conformational change that could expose a key residue (R180) for binding to laminin-1, suggesting important structural factors in their interaction.
Article Abstract
The 37/67-kDa human laminin receptor(LamR) is a cell surface protein that interacts with molecules located in the extra-cellular matrix. In particular, interactions between LamR and laminins play a major role in mediating changes in the cellular environment that affect cell adhesion, neurite outgrowth, tumor growth and metastasis. The exact interaction mode of laminin-1 and LamR is not fully understood. Laminin-1 is thought to bind to LamR through interaction with the so-called peptide G (residues 161–180) and the C-terminal helix (residues 205–229). Here we performed 100-ns atomistic force field based molecular dynamics simulations to explore the structure and dynamics of LamR related to laminin-1 interactions. Our main finding is that loop 188–197 in the C-terminal region is highly flexible. It undergoes a major change resulting in a conformational switch that partially solvent exposes the R180 residue in the final part of the G peptide. So, R180 could contribute to laminin-1 binding. Projection of the simulations along the first two principal components also confirms the importance of this conformational switch in the LamR. This may be a basic prerequisite to clarify the key structural determinants of the interaction of LamR with laminin-1.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s00249-012-0793-9 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Fluorescent aptasensor based on target-induced hairpin conformation switch coupled with nicking enzyme-assisted signal amplification for detection of beta-amyloid oligomers in cerebrospinal fluid.
Mikrochim Acta
January 2025
Department of Chemistry and Biochemistry, National Chung Cheng University, 621301, Chia-Yi, Taiwan.
A fluorescent aptasensor was developed based on target-induced hairpin conformation switch coupled with nicking enzyme-assisted signal amplification (NESA) to detect the oligomeric form of ß-amyolid peptide (AβO) in cerebrospinal fluid. The hairpin DNA probe (HP) was specifically designed to recognize AβO. When AβO is present in the sensing system, it induces an HP conformational switch and triggers the NESA reaction.
View Article and Find Full Text PDFPaxillin (PXN) and focal adhesion kinase (FAK) are two major components of the focal adhesion complex, a multiprotein structure linking the intracellular cytoskeleton to the cell exterior. PXN interacts directly with the C-terminal targeting domain of FAK (FAT) via its intrinsically disordered N-terminal domain. This interaction is necessary and sufficient for localizing FAK to focal adhesions.
View Article and Find Full Text PDFAlphaFold2 (AF2), a deep-learning based model that predicts protein structures from their amino acid sequences, has recently been used to predict multiple protein conformations. In some cases, AF2 has successfully predicted both dominant and alternative conformations of fold-switching proteins, which remodel their secondary and tertiary structures in response to cellular stimuli. Whether AF2 has learned enough protein folding principles to reliably predict alternative conformations outside of its training set is unclear.
View Article and Find Full Text PDFLight sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural-functional dynamics and biotechnological prospects.
Arch Microbiol
January 2025
Department of Botany, CMS College Kottayam, Kottayam, Kerala, 686001, India.
Among all photosynthetic life forms, cyanobacteria exclusively possess a water-soluble, light-sensitive carotenoprotein complex known as orange carotenoid proteins (OCPs), crucial for their photoprotective mechanisms. These protein complexes exhibit both structural and functional modularity, with distinct C-terminal (CTD) and N-terminal domains (NTD) serving as light-responsive sensor and effector regions, respectively. The majority of cyanobacterial genomes contain genes for OCP homologs and related proteins, highlighting their essential role in survival of the organism over time.
View Article and Find Full Text PDFConformational switches in human RNA binding proteins involved in neurodegeneration.
Biochim Biophys Acta Gen Subj
January 2025
Computational Structural Biology Laboratory, Department of Bioscience and Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India; Bioinformatics Centre, Department of Bioscience and Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India. Electronic address:
Conformational switching in RNA binding proteins (RBPs) are crucial for regulation of RNA processing and transport. Dysregulation or mutations in RBPs and broad RNA processing abnormalities are related to many human diseases including neurodegenerative disorders. Here, we review the role of protein-RNA conformational switches in RBP-RNA complexes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!