The single Asp53-Pro54 bond of the MTX2 toxin from the mamba snake Dendroaspis angusticeps is rapidly and efficiently cleaved in acidic solution (pH 1.5-2.5) at 45 degrees C. Unfolding of the toxin slows down the cleavage reaction by several times. Modelling studies indicate that the native toxin conformation can catalyse the Asp53-Pro54 bond cleavage. The implications of this study are: (i) cleavage of Asp-Pro bond for sequence determination may occur better in absence than in presence of denaturant, (ii) mild acid conditions, commonly used in NMR structure determinations, may irreversibly affect the structural integrity of Asp-Pro containing peptides and proteins.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/0014-5793(95)00844-y | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Methods for Intracellular Peptidomic Analysis.
Methods Mol Biol
April 2024
Department of Pharmacology, Biomedical Sciences Institute, University of São Paulo, São Paulo, SP, Brazil.
Peptides have broad biological significance among different species. Intracellular peptides are considered a particular class of bioactive peptides, whose generation is initiated by proteasomal degradation of cytosolic, nuclear, or mitochondrial proteins. To extract and purify intracellular peptides, which may apply for biological peptides in general, it is important to consider the initial source: tissue, cell, or fluid.
View Article and Find Full Text PDFVWD domain stabilization by autocatalytic Asp-Pro cleavage.
Protein Sci
March 2024
Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Domains known as von Willebrand factor type D (VWD) are found in extracellular and cell-surface proteins including von Willebrand factor, mucins, and various signaling molecules and receptors. Many VWD domains have a glycine-aspartate-proline-histidine (GDPH) amino-acid sequence motif, which is hydrolytically cleaved post-translationally between the aspartate (Asp) and proline (Pro). The Fc IgG binding protein (FCGBP), found in intestinal mucus secretions and other extracellular environments, contains 13 VWD domains, 11 of which have a GDPH cleavage site.
View Article and Find Full Text PDFCharacterisation of Elevenin-Vc1 from the Venom of : A Structural Analogue of α-Conotoxins.
Mar Drugs
January 2023
Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia.
Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail ( , , 11-18).
View Article and Find Full Text PDFA midposition NOTCH3 truncation in inherited cerebral small vessel disease may affect the protein interactome.
J Biol Chem
January 2023
Department of Neurology, University of Michigan, Ann Arbor, Michigan, USA; Neurology Service, VA Ann Arbor Healthcare System, Ann Arbor, Michigan, USA; Molecular and Integrative Physiology, University of Michigan, Ann Arbor, Michigan, USA. Electronic address:
Article Synopsis
- Mutations in a protein called NOTCH3 are linked to a brain disease called CADASIL, which affects small blood vessels in the brain.
- Scientists found a new way that this NOTCH3 protein can be cut up inside the body, focusing on a specific part called Asp964.
- This cutting process seems important for how NOTCH3 interacts with other proteins and might help explain how the disease works.
Hydrolysis of a second Asp-Pro site at the N-terminus of NOTCH3 in inherited vascular dementia.
Sci Rep
August 2021
Department of Neurology, University of Michigan, 7725 Medical Science Building II Box 5622, 1137 Catherine St., Ann Arbor, MI, 48109-5622, USA.
Cerebrovascular pathology at the biochemical level has been informed by the study of cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL), a vascular disorder caused by NOTCH3 mutations. Previous work in CADASIL described N-terminal proteolysis of NOTCH3 generated by specific non-enzymatic cleavage of the first Asp-Pro sequence of the protein. Here, we investigated whether the second Asp-Pro peptide bond (residues 121-122) of NOTCH3 is cleaved in CADASIL.
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!