1k9k

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(New page: 200px<br /> <applet load="1k9k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k9k, resolution 1.76&Aring;" /> '''CRYSTAL STRUCTURE O...)
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caption="1k9k, resolution 1.76&Aring;" />
'''CRYSTAL STRUCTURE OF CALCIUM BOUND HUMAN S100A6'''<br />
'''CRYSTAL STRUCTURE OF CALCIUM BOUND HUMAN S100A6'''<br />
==Overview==
==Overview==
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S100A6 is a member of the S100 family of Ca(2+) binding proteins, which, have come to play an important role in the diagnosis of cancer due to, their overexpression in various tumor cells. We have determined the, crystal structures of human S100A6 in the Ca(2+)-free and Ca(2+)-bound, states to resolutions of 1.15 A and 1.44 A, respectively. Ca(2+) binding, is responsible for a dramatic change in the global shape and charge, distribution of the S100A6 dimer, leading to the exposure of two, symmetrically positioned target binding sites. The results are consistent, with S100A6, and most likely other S100 proteins, functioning as Ca(2+), sensors in a way analogous to the prototypical sensors calmodulin and, troponin C. The structures have important implications for our, understanding of target binding and cooperativity of Ca(2+) binding in the, S100 family.
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S100A6 is a member of the S100 family of Ca(2+) binding proteins, which have come to play an important role in the diagnosis of cancer due to their overexpression in various tumor cells. We have determined the crystal structures of human S100A6 in the Ca(2+)-free and Ca(2+)-bound states to resolutions of 1.15 A and 1.44 A, respectively. Ca(2+) binding is responsible for a dramatic change in the global shape and charge distribution of the S100A6 dimer, leading to the exposure of two symmetrically positioned target binding sites. The results are consistent with S100A6, and most likely other S100 proteins, functioning as Ca(2+) sensors in a way analogous to the prototypical sensors calmodulin and troponin C. The structures have important implications for our understanding of target binding and cooperativity of Ca(2+) binding in the S100 family.
==About this Structure==
==About this Structure==
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1K9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K9K OCA].
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1K9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9K OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]
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[[Category: Otterbein, L.R.]]
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[[Category: Otterbein, L R.]]
[[Category: BME]]
[[Category: BME]]
[[Category: CA]]
[[Category: CA]]
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[[Category: s100a6]]
[[Category: s100a6]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:48:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:37 2008''

Revision as of 11:31, 21 February 2008

Image:1k9k.gif

1k9k, resolution 1.76Å

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CRYSTAL STRUCTURE OF CALCIUM BOUND HUMAN S100A6

Overview

S100A6 is a member of the S100 family of Ca(2+) binding proteins, which have come to play an important role in the diagnosis of cancer due to their overexpression in various tumor cells. We have determined the crystal structures of human S100A6 in the Ca(2+)-free and Ca(2+)-bound states to resolutions of 1.15 A and 1.44 A, respectively. Ca(2+) binding is responsible for a dramatic change in the global shape and charge distribution of the S100A6 dimer, leading to the exposure of two symmetrically positioned target binding sites. The results are consistent with S100A6, and most likely other S100 proteins, functioning as Ca(2+) sensors in a way analogous to the prototypical sensors calmodulin and troponin C. The structures have important implications for our understanding of target binding and cooperativity of Ca(2+) binding in the S100 family.

About this Structure

1K9K is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution., Otterbein LR, Kordowska J, Witte-Hoffmann C, Wang CL, Dominguez R, Structure. 2002 Apr;10(4):557-67. PMID:11937060

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