The relation between the divergence of sequence and structure in proteins.

By Cyrus Chothia, Arthur M. Lesk. 1986

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Citations in the corpus

Toward the estimation of the absolute quality of individual protein structure models (2010, background): “However, with decreasing sequence similarity, an increasing amount of structural divergence is observed (Chothia and Lesk, 1986; Rost, 1999), and the resulting models may contain significant inaccuracies, especially models built on distant templates.”
Phaser crystallographic software (2007, methodology): “Although the first of these (high completeness) can be determined in advance from the fraction of the total molecular weight represented by the model, the second can only be estimated from the Chothia & Lesk (1986) formula and the third is unknown in advance.”
The Protein Model Portal—a comprehensive resource for protein structure and model information (2013, methodology): “Expected quality of the model based on the sequence identity between aligned target and template sequences is illustrated in panel III, where a vertical red bar marks the sequence identity of 27% to the template and the expected model accuracy based on the work of Chothia and Lesk (37).”
Comparative protein structure modeling of genes and genomes. (2000, background): “The reasons are the well-known relationship between structural and sequence similarities of two proteins (34), the ‘geometrical’ nature of modeling that forces the model to be as close to the template as possible A nn u.”
Structure is three to ten times more conserved than sequence—A study of structural response in protein cores (2009, result): “The well-known exponential relation between RMSD and sequence identity, ID,11 can also be seen in our data [Fig.”
The protein folding problem. (2008, unknown): “A key advance was the exploitation of evolutionary relationships among sequences through the development of robust sequence alignment methods (32,64,224).”
Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. (2005, background): “With a few notable exceptions (Dalal et al., 1997; Gerstein and Levitt, 1998; Riesner, 2003), a clear amino acid sequence relationship between two proteins implies that they have similar structure (Chothia and Lesk, 1986).”
Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection (2014, methodology): “simulating a Potts model with the Potts variables representing the possible amino acid types being placed on the sites in a representative average native structure, because 3D native structure is largely conserved (9, 17).”
Automated Protein Structure Modeling with SWISS-MODEL Workspace and the Protein Model Portal (2012, background): “…expected quality of a structural model is the sequence identity between the target and the template sequences, where in general higher sequence similarity leads to more accurate models since the evolutionary structural divergence will be smaller (39) and alignment errors less likely to occur (40).”
Coevolutionary Analysis of Protein Subfamilies by Sequence Reweighting (2019, background): “While such structural models are of great value, they might actually represent “snapshots” of the heterogeneous structural ensemble characterizing the complete protein family [20].”