2hda: Difference between revisions
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==Overview== | ==Overview== | ||
SH3 domains from the Src family of tyrosine kinases represent an | SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. The development of inhibitors of therapeutic potential requires a good understanding of the molecular determinants of binding affinity and specificity and relies on the availability of high quality structural information. Here, we present the first high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, we present here the first report of amyloid aggregation by an SH3 domain from the Src family. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: | Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation., Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A, FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17418139 17418139] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific protein-tyrosine kinase]] | [[Category: Non-specific protein-tyrosine kinase]] | ||
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[[Category: Camara-Artigas, A.]] | [[Category: Camara-Artigas, A.]] | ||
[[Category: Luque, I.]] | [[Category: Luque, I.]] | ||
[[Category: Martin-Garcia, J | [[Category: Martin-Garcia, J M.]] | ||
[[Category: Mateo, P | [[Category: Mateo, P L.]] | ||
[[Category: Ruiz-Sanz, J.]] | [[Category: Ruiz-Sanz, J.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: main beta]] | [[Category: main beta]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:38 2008'' | ||
Revision as of 18:40, 21 February 2008
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Yes SH3 domain
OverviewOverview
SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. The development of inhibitors of therapeutic potential requires a good understanding of the molecular determinants of binding affinity and specificity and relies on the availability of high quality structural information. Here, we present the first high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, we present here the first report of amyloid aggregation by an SH3 domain from the Src family.
About this StructureAbout this Structure
2HDA is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Non-specific protein-tyrosine kinase, with EC number 2.7.10.2 Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation., Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A, FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:17418139
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