1rja
From Proteopedia
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'''Solution Structure and Backbone Dynamics of the Nonreceptor Tyrosine Kinase PTK6/Brk SH2 Domain'''<br /> | '''Solution Structure and Backbone Dynamics of the Nonreceptor Tyrosine Kinase PTK6/Brk SH2 Domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http:// | + | 1RJA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RJA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: src homology 2(sh2) domain]] | [[Category: src homology 2(sh2) domain]] | ||
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Revision as of 14:48, 15 February 2008
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Solution Structure and Backbone Dynamics of the Nonreceptor Tyrosine Kinase PTK6/Brk SH2 Domain
Contents |
Overview
Human protein-tyrosine kinase-6 (PTK6, also known as breast tumor kinase, (Brk)) is a member of the non-receptor protein-tyrosine kinase family and, is expressed in two-thirds of all breast tumors. To understand the, structural basis of PTK6 function, we have determined the solution, structure and backbone dynamics of the PTK6-Src homology 2 (SH2) domain, using multidimensional NMR spectroscopy. The solution structure clearly, indicates that the SH2 domain of human PTK6 contains a consensus, alpha/beta-fold and a Tyr(P) peptide binding surface, which are common to, other SH2 domains. However, two of the alpha-helices (alphaA and alphaB), are located on opposite faces of the central beta-sheet. In addition, the, topological arrangement of a central four-stranded antiparallel beta-sheet, (strands betaA, betaB, betaC, and betaD) differs from that of other Src, family members. Backbone dynamics and Tyr(P) peptide titration experiments, revealed that the putative ligand binding sites of the PTK6-SH2 domain, undergo distinctive internal motions when compared with other regions of, the protein. Surface plasmon resonance analysis showed that the Tyr(P), peptide had a dissociation constant of about 60 microm, which is, substantially weaker binding than previously reported for Src family, members. The solution structure together with data from the ligand binding, mode of PTK6-SH2 provides insight into the molecular basis of the, autoinhibitory role of PTK6.
Disease
Known disease associated with this structure: Bruck syndrome OMIM:[259450]
About this Structure
1RJA is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Solution structure and backbone dynamics of the non-receptor protein-tyrosine kinase-6 Src homology 2 domain., Hong E, Shin J, Kim HI, Lee ST, Lee W, J Biol Chem. 2004 Jul 9;279(28):29700-8. Epub 2004 Mar 31. PMID:15056653
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