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Binding of a C-end rule peptide to the neuropilin-1 receptor: a molecular modeling approach
dc.contributor.author | Haspel, Nurit |
dc.contributor.author | Zanuy Gomara, David |
dc.contributor.author | Nussinov, Ruth |
dc.contributor.author | Teesalu, Tambet |
dc.contributor.author | Ruoslahti, Erkki |
dc.contributor.author | Alemán Llansó, Carlos |
dc.contributor.other | Universitat Politècnica de Catalunya. Departament d'Enginyeria Química |
dc.date.accessioned | 2011-08-30T10:41:38Z |
dc.date.available | 2011-08-30T10:41:38Z |
dc.date.created | 2011-03-15 |
dc.date.issued | 2011-03-15 |
dc.identifier.citation | Haspel [et al.]. Binding of a C-end rule peptide to the neuropilin-1 receptor: a molecular modeling approach. "Biochemistry", 15 Març 2011, vol. 50, núm. 10, p. 1755-1762. |
dc.identifier.issn | 0006-2960 |
dc.identifier.uri | http://hdl.handle.net/2117/13140 |
dc.description.abstract | Neuropilin-1 (NRP-1) is a receptor that plays an essential role in angiogenesis, vascular permeability, and nervous system development. Previous studies have shown that peptides with an N-terminal Arg, especially peptides with the four-residue consensus sequence R/K/XXR/K, bind to NRP-1 cell surfaces. Peptides containing such consensus sequences promote binding and internalization into cells, while blocking the C-terminal Arg (or Lys) prevents the internalization. In this study, we use molecular dynamics simulations to model the structural properties of the NRP-1 complex with a prototypic CendR peptide, RPAR. Our simulations show that RPAR binds NRP-1 through specific interactions of the RPAR C-terminus: three hydrogen bonds and a salt bridge anchor the ligand in the receptor pocket. The modeling results were used as the starting point for a systematic computational study of new RPAR analogues based on chemical modifications of their natural amino acids. Comparison of the structural properties of the new peptide-receptor complexes with the original organization suggests that some of the analogues can increase the binding affinity while reducing the natural sensitivity of RXXR to endogenous proteases. |
dc.format.extent | 8 p. |
dc.language.iso | eng |
dc.subject | Àrees temàtiques de la UPC::Enginyeria química::Química física::Estructura molecular |
dc.subject.lcsh | Neuropilin-1 |
dc.title | Binding of a C-end rule peptide to the neuropilin-1 receptor: a molecular modeling approach |
dc.type | Article |
dc.subject.lemac | Neuropilina-1 |
dc.contributor.group | Universitat Politècnica de Catalunya. IMEM - Innovació, Modelització i Enginyeria en (BIO) Materials |
dc.identifier.doi | 10.1021/bi101662j |
dc.description.peerreviewed | Peer Reviewed |
dc.relation.publisherversion | http://www.ncbi.nlm.nih.gov/pubmed/21247217 |
dc.rights.access | Restricted access - publisher's policy |
local.identifier.drac | 5432597 |
dc.description.version | Postprint (published version) |
local.citation.author | Haspel; Zanuy, D.; Nussinov, R.; Teesalu, T.; Ruoslahti, E.; Alemán, C. |
local.citation.publicationName | Biochemistry |
local.citation.volume | 50 |
local.citation.number | 10 |
local.citation.startingPage | 1755 |
local.citation.endingPage | 1762 |
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