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Journal ArticleDOI

Network analysis of protein structures identifies functional residues.

TLDR
This work transformed protein structures into residue interaction graphs (RIGs), where amino acid residues are graph nodes and their interactions with each other are the graph edges, and found that active site, ligand-binding and evolutionary conserved residues, typically have high closeness values.
About
This article is published in Journal of Molecular Biology.The article was published on 2004-12-03. It has received 463 citations till now. The article focuses on the topics: Protein structure & Active site.

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Citations
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Automated protein function prediction—the genomic challenge

TL;DR: The history of automated protein function prediction, a need for a functional annotation which is standardized and machine readable so that function prediction programs could be incorporated into larger workflows, and the latest innovations in all three topics are surveyed.
Journal ArticleDOI

A Network Representation of Protein Structures: Implications for Protein Stability

TL;DR: The hubs identified are found to play a role in bringing together different secondary structural elements in the tertiary structure of the proteins, and could be crucial for the folding and stability of the unique three-dimensional structure of proteins.
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Predicting protein ligand binding sites by combining evolutionary sequence conservation and 3D structure.

TL;DR: ConCavity is introduced, a small molecule binding site prediction algorithm that integrates evolutionary sequence conservation estimates with structure-based methods for identifying protein surface cavities and finds that the two approaches provide largely complementary information, which can be combined to improve upon either approach alone.
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Residues crucial for maintaining short paths in network communication mediate signaling in proteins.

TL;DR: It is proposed that centrally conserved residues, whose removal increases the characteristic path length in protein networks, may relate to the system fragility.
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Predicting protein function from sequence and structural data.

TL;DR: Several automated servers that integrate evidence from multiple sources have been released this year and particular improvements have been seen with methods utilizing the Gene Ontology functional annotation schema.
References
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Book

Small World

Martin Suter
Journal ArticleDOI

An evolutionary trace method defines binding surfaces common to protein families

TL;DR: The evolutionary trace method is a systematic, transparent and novel predictive technique that identifies active sites and functional interfaces in proteins with known structure and provides an evolutionary perspective for judging the functional or structural role of each residue in protein structure.
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ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information

TL;DR: A new web server, ConSurf, is presented, which automates algorithms for the identification of functionally important regions in proteins of known three dimensional structure by estimating the degree of conservation of the amino-acid sites among their close sequence homologues.
Journal ArticleDOI

Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase

TL;DR: It is demonstrated that MAP kinase is only active when both tyrosyl and threonyl residues are phosphorylated and suggested therefore that the enzyme functions in vivo to integrate signals from two distinct transduction pathways.
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