NDLI: The nature of the conserved basic amino acid sequences found among 437 heparin binding proteins determined by network analysis

Please wait, while we are loading the content...

Stereoselective binding of agonists to the β₂-adrenergic receptor: insights into molecular details and thermodynamics from molecular dynamics simulations

How RNase HI (Escherichia coli) promoted site-selective hydrolysis works on RNA in duplex with carba-LNA and LNA substituted antisense strands in an antisense strategy context?

Inhibition of the MurA enzyme in Fusobacterium nucleatum by potential inhibitors identified through computational and in vitro approaches

A systematic reconstruction and constraint-based analysis of Leishmania donovani metabolic network: identification of potential antileishmanial drug targets

Aggregation behavior of novel heptamethine cyanine dyes upon their binding to native and fibrillar lysozyme

Structural modeling of the AhR:ARNT complex in the bHLH–PASA–PASB region elucidates the key determinants of dimerization

Integrating multiple omics data for the discovery of potential Beclin-1 interactions in breast cancer

Small molecule induced poly(A) single strand to self-structure conformational switching: evidence for the prominent role of H-bonding interactions

A structural bioinformatics investigation on protein–DNA complexes delineates their modes of interaction

An integrated anti-arrhythmic target network of a Chinese medicine compound, Wenxin Keli, revealed by combined machine learning and molecular pathway analysis

An all-atom molecular dynamics study of the anti-interferon signaling of Ebola virus: interaction mechanisms of EBOV VP24 binding to Karyopherin alpha5

Back cover

Molecular BioSystems Vol - 13 Issue - 4

Molecular BioSystems Vol - 13 Issue - 3

Molecular BioSystems Vol - 13 Issue - 2

Molecular BioSystems Vol - 13 Issue - 1

Molecular BioSystems Vol -12

Molecular BioSystems Vol -9

Molecular BioSystems Vol -8

Molecular BioSystems Vol -7

Molecular BioSystems Vol -6

Molecular BioSystems Vol -5

Molecular BioSystems Vol -4

Molecular BioSystems Vol -3

Molecular BioSystems Vol -2

The nature of the conserved basic amino acid sequences found among 437 heparin binding proteins determined by network analysis

Content Provider	Royal Society of Chemistry (RSC)
Author	Preston, Mark D. Yates, Edwin A. Rudd, Timothy R.
Copyright Year	2017
Abstract	In multicellular organisms, a large number of proteins interact with the polyanionic polysaccharides heparan sulphate (HS) and heparin. These interactions are usually assumed to be dominated by charge–charge interactions between the anionic carboxylate and/or sulfate groups of the polysaccharide and cationic amino acids of the protein. A major question is whether there exist conserved amino acid sequences for HS/heparin binding among these diverse proteins. Potentially conserved HS/heparin binding sequences were sought amongst 437 HS/heparin binding proteins. Amino acid sequences were extracted and compared using a Levenshtein distance metric. The resultant similarity matrices were visualised as graphs, enabling extraction of strongly conserved sequences from highly variable primary sequences while excluding short, core regions. This approach did not reveal extensive, conserved HS/heparin binding sequences, rather a number of shorter, more widely spaced sequences that may work in unison to form heparin-binding sites on protein surfaces, arguing for convergent evolution. Thus, it is the three-dimensional arrangement of these conserved motifs on the protein surface, rather than the primary sequence per se, which are the evolutionary elements.
Starting Page	852
Ending Page	865
Page Count	14
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	13
Issue Number	5
Journal	Molecular BioSystems
DOI	10.1039/c6mb00857g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Heparan sulfate Interaction Heparin Sulfate Levenshtein distance Convergent evolution Polysaccharide Protein
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

A Systems Biology Approach for the Investigation of the Heparin/Heparan Sulfate Interactome

Demystifying Heparan Sulfate–Protein Interactions

Heparan sulfates and heparan sulfate binding proteins in sepsis

Interaction of heparin and heparin-derived oligosaccharides with synthetic peptide analogues of the heparin-binding domain of heparin/heparan sulfate-interacting protein☆

Recombinant Heparin—New Opportunities

Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein.

Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes.

The amino acid sequences of the carboxyl termini of human and mouse hepatic lipase influence cell surface association

Conserved amino acid sequences among plant proteins sorted to protein bodies and plant vacuoles. Can they play a role in protein sorting?

The nature of the conserved basic amino acid sequences found among 437 heparin binding proteins determined by network analysis

Similar Documents

A Systems Biology Approach for the Investigation of the Heparin/Heparan Sulfate Interactome

Demystifying Heparan Sulfate–Protein Interactions

Heparan sulfates and heparan sulfate binding proteins in sepsis

Interaction of heparin and heparin-derived oligosaccharides with synthetic peptide analogues of the heparin-binding domain of heparin/heparan sulfate-interacting protein☆

Recombinant Heparin—New Opportunities

Heparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein.

Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes.

The amino acid sequences of the carboxyl termini of human and mouse hepatic lipase influence cell surface association

Conserved amino acid sequences among plant proteins sorted to protein bodies and plant vacuoles. Can they play a role in protein sorting?

The nature of the conserved basic amino acid sequences found among 437 heparin binding proteins determined by network analysis