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InterProSurf specifications


Unique identifier OMICS_08136
Name InterProSurf
Interface Web user interface
Restrictions to use None
Input data Macromolecular structure data
Input format PDB
Computer skills Basic
Stability Stable
Maintained Yes

Publication for InterProSurf

InterProSurf citations


Linear epitope prediction in HPV type 16 E7 antigen and their docked interaction with human TMEM 50A structural model

PMCID: 5498776
PMID: 28690376
DOI: 10.6026/97320630013122

[…] InterProSurf was used for protein-protein interactions studies of the docked molecules, which investigated the role of hydrogen bond formation, hydrophobic residues and overall electrostatics with tot […]


Superficial vimentin mediates DENV 2 infection of vascular endothelial cells

Sci Rep
PMCID: 5133558
PMID: 27910934
DOI: 10.1038/srep38372

[…] he docking complex with the pairwise shape complementarity, desolvation, and electrostatic energy methods. The interaction residues of the vimentin rod and DENV-2 EDIII proteins were predicted by the InterproSurf software, and an interacting interface was analyzed by the Pymol 1.7.3 software. […]


Structural Dynamics Investigation of Human Family 1 and 2 Cystatin Cathepsin L1 Interaction: A Comparison of Binding Modes

PLoS One
PMCID: 5072729
PMID: 27764212
DOI: 10.1371/journal.pone.0164970

[…] CASTp (Computed Atlas of Surface Topology of proteins) [], cons-PPISP (consensus–Protein–Protein Interaction Site Predictor) [] and the InterProSurf server [] were utilized to locate the binding-sites in prepared PDB files. To find out the binding modes of cathepsin-cystatin/stefin complexes, crystallographic and modeled structures of […]


Molecular dynamics simulations and docking enable to explore the biophysical factors controlling the yields of engineered nanobodies

Sci Rep
PMCID: 5056509
PMID: 27721441
DOI: 10.1038/srep34869

[…] rresponded to the internal residue Arg35 next to the mutation Phe34 → Val. As a complementary approach, we analyzed each reference conformation with the web-tool protein-protein interaction predictor Interprosurf to identify the hydrophobic solvent-accessible residues, prone to interact with other protein groups. We then represented the residues selected from both approaches (see ) and we grouped […]


Prediction of Protein Protein Interaction Sites Based on Naive Bayes Classifier

PMCID: 4677168
PMID: 26697220
DOI: 10.1155/2015/978193

[…] accessibility (SA) that exceeded 1.0 Å2 compared to that in the monomer formation. An amino acid residue was classified to be either interface class or noninterface. In this paper we used web server InterProSurf available at website to determine the interface residue of protein complexes from its PDB number. Dset186 consists of 36219 residues of which 4241 (1 […]


Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter

PMCID: 4662854
PMID: 26341627
DOI: 10.15252/embr.201540436

[…] ounded by hydrophilic residues (namely D142, D166 and E171) (Fig F). This surface and C‐terminus tail (174ATLNNVKTL182) were predicted as potential protein–protein interaction (PPI) interfaces by the InterProSurf analysis (Fig A and C) and the consensus Protein–Protein Interaction Site Predictor (cons‐PPISP) server (Fig B and C). In the crystals of T4 lysozyme‐MCU NTD and MCU NTD‐E, MCU NTDs for […]


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InterProSurf institution(s)
Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX, USA

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