NDLI: Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.

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

Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.

Site2 binding energetics of the regulatory step of growth hormone-induced receptor homodimerization.

The solution structure of bovine pancreatic trypsin inhibitor at high pressure.

Dissecting interdomain communication within cAPK regulatory subunit type IIbeta using enhanced amide hydrogen/deuterium exchange mass spectrometry (DXMS).

Efficient biosynthetic incorporation of tryptophan and indole analogs in an integral membrane protein.

A graph-theory algorithm for rapid protein side-chain prediction.

Rationally selected basis proteins: A new approach to selecting proteins for spectroscopic secondary structure analysis

Discrete restraint-based protein modeling and the Calpha-trace problem.

Opposing effects of phosphoenolpyruvate and pyruvate with $Mg^{2+}$ on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli

Contact order revisited: influence of protein size on the folding rate.

Prospects and limitations of the rational engineering of fibrillar collagens.

Refolding out of guanidine hydrochloride is an effective approach for high-throughput structural studies of small proteins.

Structure-activity relationships in HIV-1 reverse transcriptase revealed by radiation target analysis.

Phosphohydrolase and transphosphatidylation reactions of two Streptomyces phospholipase D enzymes: Covalent versus noncovalent catalysis

Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.

Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.

Lipid-binding proteins: structure of the phospholipid ligands.

Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.

Year: 2003 Volume: 12 Issue: 8

Year: 2003 Volume: 12 Issue: 7

Year: 2003 Volume: 12 Issue: 6

Year: 2003 Volume: 12 Issue: 5

Year: 2003 Volume: 12 Issue: 4

Year: 2003 Volume: 12 Issue: 3

Year: 2003 Volume: 12 Issue: 2

Year: 2003 Volume: 12 Issue: 1

Year: 2002 Volume: 11

Year: 2001 Volume: 10

Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Westhead, David R. Bradford, James R.
Description	Country affiliation: United kingdom Author Affiliation: Bradford JR ( School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK.)
Abstract	We have carried out a thorough and systematic sequence-structure study on how the pattern of conservation at the interface differs from the noninteracting surface in seven proteases and their inhibitors. As expected, the interface of a protease could be easily distinguished from the noninteracting surface by a concentrated area of conservation. In contrast, there was less distinction to be made between the interface and the noninteracting surface of inhibitors, and in five of the seven cases, a higher proportion of the interface area was variable compared to the rest of the surface. This is likely to cause a problem for binding-site prediction methods that assume the largest cluster of highly conserved residues on the surface of a protein corresponds to the interface. We conclude that such methods would succeed when applied to our protease test cases, but complications could arise with the inhibitors. These results also impact on methods to solve the protein-protein docking problem that use conservation at the interface to provide the location of the two protein binding sites prior to application of the docking algorithm.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	12
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2003-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Enzyme Inhibitors Chemistry Enzymes Genetics Mutation Proteomics Algorithms Computational Biology Databases As Topic Endopeptidases Evolution, Molecular Protein Binding Proteins Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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

Asymmetric mutation rates at enzyme–inhibitor interfaces: Implications for the protein–protein docking problem

Interolog interfaces in protein-protein docking.

The dataset for protein-RNA binding affinity.

Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: implications for the protein docking problem.

A new, structurally nonredundant, diverse data set of protein-protein interfaces and its implications.

Docking by structural similarity at protein-protein interfaces.

Blind predictions of protein interfaces by docking calculations in CAPRI.

Protein docking using case-based reasoning.

TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.

Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.

Similar Documents

Asymmetric mutation rates at enzyme–inhibitor interfaces: Implications for the protein–protein docking problem

Interolog interfaces in protein-protein docking.

The dataset for protein-RNA binding affinity.

Comparison of protein-protein interactions in serine protease-inhibitor and antibody-antigen complexes: implications for the protein docking problem.

A new, structurally nonredundant, diverse data set of protein-protein interfaces and its implications.

Docking by structural similarity at protein-protein interfaces.

Blind predictions of protein interfaces by docking calculations in CAPRI.

Protein docking using case-based reasoning.

TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.

Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.