دورية أكاديمية
أعرض في EDS

Rational design of new binding specificity by simultaneous mutagenesis of calmodulin and a target peptide.

التفاصيل البيبلوغرافية
العنوان: Rational design of new binding specificity by simultaneous mutagenesis of calmodulin and a target peptide.
المؤلفون: Green DF; Biological Engineering Division, Computer Science and Artificial Intelligence Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307, USA., Dennis AT, Fam PS, Tidor B, Jasanoff A
المصدر: Biochemistry [Biochemistry] 2006 Oct 17; Vol. 45 (41), pp. 12547-59.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Print ISSN: 0006-2960 (Print) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, American Chemical Society.
مواضيع طبية MeSH: Calmodulin/*genetics , Calmodulin/*metabolism , Calmodulin-Binding Proteins/*genetics , Calmodulin-Binding Proteins/*metabolism , Peptides/*genetics , Peptides/*metabolism, Amino Acid Sequence ; Animals ; Calcium Signaling ; Calmodulin/chemistry ; Calmodulin-Binding Proteins/chemistry ; Drug Design ; In Vitro Techniques ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Myosin-Light-Chain Kinase/chemistry ; Myosin-Light-Chain Kinase/genetics ; Myosin-Light-Chain Kinase/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Peptides/chemistry ; Protein Binding ; Protein Conformation ; Protein Engineering ; Protein Structure, Tertiary ; Rabbits ; Thermodynamics
مستخلص: Calcium-saturated calmodulin (CaM) binds and influences the activity of a varied collection of target proteins in most cells. This promiscuity underlies the role of CaM as a shared participant in calcium-dependent signal transduction pathways but imposes a handicap on popular CaM-based calcium biosensors, which display an undesired tendency to cross-react with cellular proteins. Designed CaM/target pairs that retain high affinity for one another but lack affinity for wild-type CaM and its natural interaction partners would therefore be useful as sensor components and possibly also as elements of "synthetic" cellular-signaling networks. Here, we have adopted a rational approach to creating suitably modified CaM/target complexes by using computational design methods to guide parallel site-directed mutagenesis of both binding partners. A hierarchical design procedure was applied to suggest a small number of complementary mutations on CaM and on a peptide ligand derived from skeletal-muscle light-chain kinase (M13). Experimental analysis showed that the procedure was successful in identifying CaM and M13 mutants with novel specificity for one another. Importantly, the designed complexes retained an affinity comparable to the wild-type CaM/M13 complex. These results represent a step toward the creation of CaM and M13 derivatives with specificity fully orthogonal to the wild-type proteins and show that qualitatively accurate predictions may be obtained from computational methods applied simultaneously to two proteins involved in multiple-linked binding equilibria.
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معلومات مُعتمدة: R01 GM065418-02 United States GM NIGMS NIH HHS; R21 EB005723 United States EB NIBIB NIH HHS; R56 GM065418 United States GM NIGMS NIH HHS; GM065418 United States GM NIGMS NIH HHS; R01 GM065418 United States GM NIGMS NIH HHS; EB005723 United States EB NIBIB NIH HHS
المشرفين على المادة: 0 (Calmodulin)
0 (Calmodulin-Binding Proteins)
0 (M13 protein (myosin light-chain kinase))
0 (Peptide Fragments)
0 (Peptides)
EC 2.7.11.18 (Myosin-Light-Chain Kinase)
تواريخ الأحداث: Date Created: 20061013 Date Completed: 20061108 Latest Revision: 20181113
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC2517080
DOI: 10.1021/bi060857u
PMID: 17029410
قاعدة البيانات: MEDLINE
الوصف
تدمد:0006-2960
DOI:10.1021/bi060857u