1ul7

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(New page: 200px<br /><applet load="1ul7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ul7" /> '''Solution structure of kinase associated doma...)
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'''Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3'''<br />
'''Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3'''<br />
==Overview==
==Overview==
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Microtubule-associated protein/microtubule affinity-regulating kinases, (MARKs)/PAR-1 are common regulators of cell polarity that are conserved, from nematode to human. All of these kinases have a highly conserved, C-terminal domain, which is termed the kinase-associated domain 1 (KA1), although its function is unknown. In this study, we determined the, solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy., We found that approximately 50 additional residues preceding the, previously defined KA1 domain are required for its proper folding. The, newly defined KA1 domain adopts a compact alpha+beta structure with a, betaalphabetabetabetabetaalpha topology. We also found a characteristic, hydrophobic, concave surface surrounded by positively charged residues., This concave surface includes the highly conserved Glu-Leu-Lys-Leu motif, at the C terminus, indicating that it is important for the function of the, KA1 domain.
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Microtubule-associated protein/microtubule affinity-regulating kinases (MARKs)/PAR-1 are common regulators of cell polarity that are conserved from nematode to human. All of these kinases have a highly conserved C-terminal domain, which is termed the kinase-associated domain 1 (KA1), although its function is unknown. In this study, we determined the solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy. We found that approximately 50 additional residues preceding the previously defined KA1 domain are required for its proper folding. The newly defined KA1 domain adopts a compact alpha+beta structure with a betaalphabetabetabetabetaalpha topology. We also found a characteristic hydrophobic, concave surface surrounded by positively charged residues. This concave surface includes the highly conserved Glu-Leu-Lys-Leu motif at the C terminus, indicating that it is important for the function of the KA1 domain.
==About this Structure==
==About this Structure==
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1UL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UL7 OCA].
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1UL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL7 OCA].
==Reference==
==Reference==
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[[Category: Kigawa, T.]]
[[Category: Kigawa, T.]]
[[Category: Koshiba, S.]]
[[Category: Koshiba, S.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Tochio, N.]]
[[Category: Tochio, N.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:13:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:41 2008''

Revision as of 13:25, 21 February 2008


1ul7

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Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3

Overview

Microtubule-associated protein/microtubule affinity-regulating kinases (MARKs)/PAR-1 are common regulators of cell polarity that are conserved from nematode to human. All of these kinases have a highly conserved C-terminal domain, which is termed the kinase-associated domain 1 (KA1), although its function is unknown. In this study, we determined the solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy. We found that approximately 50 additional residues preceding the previously defined KA1 domain are required for its proper folding. The newly defined KA1 domain adopts a compact alpha+beta structure with a betaalphabetabetabetabetaalpha topology. We also found a characteristic hydrophobic, concave surface surrounded by positively charged residues. This concave surface includes the highly conserved Glu-Leu-Lys-Leu motif at the C terminus, indicating that it is important for the function of the KA1 domain.

About this Structure

1UL7 is a Single protein structure of sequence from Mus musculus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3., Tochio N, Koshiba S, Kobayashi N, Inoue M, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Motoda Y, Kobayashi A, Tanaka A, Hayashizaki Y, Terada T, Shirouzu M, Kigawa T, Yokoyama S, Protein Sci. 2006 Nov;15(11):2534-43. PMID:17075132

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