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Surface Comparison of Active and Inactive Protein Kinases Identifies a Conserved Activation Mechanis...

Surface Comparison of Active and Inactive Protein Kinases Identifies a Conserved Activation Mechanis...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1693824

Surface Comparison of Active and Inactive Protein Kinases Identifies a Conserved Activation Mechanism

About this item

Full title

Surface Comparison of Active and Inactive Protein Kinases Identifies a Conserved Activation Mechanism

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2006-11, Vol.103 (47), p.17783-17788

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

The surface comparison of different serine-threonine and tyrosine kinases reveals a set of 30 residues whose spatial positions are highly conserved. The comparison between active and inactive conformations identified the residues whose positions are the most sensitive to activation. Based on these results, we propose a model of protein kinase activ...

Alternative Titles

Full title

Surface Comparison of Active and Inactive Protein Kinases Identifies a Conserved Activation Mechanism

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1693824

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1693824

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0607656103

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