1ggz

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(New page: 200px<br /> <applet load="1ggz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggz, resolution 1.5&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1ggz.gif|left|200px]]<br /><applet load="1ggz" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1ggz" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1ggz, resolution 1.5&Aring;" />
caption="1ggz, resolution 1.5&Aring;" />
'''CRYSTAL STRUCTURE OF THE CALMODULIN-LIKE PROTEIN (HCLP) FROM HUMAN EPITHELIAL CELLS'''<br />
'''CRYSTAL STRUCTURE OF THE CALMODULIN-LIKE PROTEIN (HCLP) FROM HUMAN EPITHELIAL CELLS'''<br />
==Overview==
==Overview==
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A calmodulin (CaM)-like protein (hCLP) is expressed in human mammary, epithelial cells but appears to be limited to certain epithelial cells, such as those found in skin, prostate, breast and cervical tissues. A, decrease in the expression of this protein is associated with the, occurrence of tumors in breast epithelium. The structure of hCLP, determined to 1.5 A resolution by X-ray crystallography shows a distinct, 30 degrees displacement along the interconnecting central helix, when, compared to the highly conserved structure of vertebrate CaM, resulting in, a difference in the relative orientation of its two globular domains., Additionally, the electric surface potential landscape at the target, protein binding regions on the two globular domains of hCLP is, significantly different from those of CaM, indicating that the respective, ranges of hCLP and hCaM target proteins do not fully overlap. Observations, that hCLP can competitively inhibit CaM activation of target proteins also, imply a role for hCLP in which it may also serve as a modulator of CaM, activity in the epithelial cells where hCLP is expressed.
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A calmodulin (CaM)-like protein (hCLP) is expressed in human mammary epithelial cells but appears to be limited to certain epithelial cells such as those found in skin, prostate, breast and cervical tissues. A decrease in the expression of this protein is associated with the occurrence of tumors in breast epithelium. The structure of hCLP determined to 1.5 A resolution by X-ray crystallography shows a distinct 30 degrees displacement along the interconnecting central helix, when compared to the highly conserved structure of vertebrate CaM, resulting in a difference in the relative orientation of its two globular domains. Additionally, the electric surface potential landscape at the target protein binding regions on the two globular domains of hCLP is significantly different from those of CaM, indicating that the respective ranges of hCLP and hCaM target proteins do not fully overlap. Observations that hCLP can competitively inhibit CaM activation of target proteins also imply a role for hCLP in which it may also serve as a modulator of CaM activity in the epithelial cells where hCLP is expressed.
==About this Structure==
==About this Structure==
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1GGZ 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GGZ OCA].
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1GGZ 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGZ OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Han, B.G.]]
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[[Category: Han, B G.]]
[[Category: Han, M.]]
[[Category: Han, M.]]
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[[Category: Jap, B.K.]]
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[[Category: Jap, B K.]]
[[Category: Sui, H.]]
[[Category: Sui, H.]]
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[[Category: Walian, P.J.]]
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[[Category: Walian, P J.]]
[[Category: Yaswen, P.]]
[[Category: Yaswen, P.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: ef hand]]
[[Category: ef hand]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:05:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:58 2008''

Revision as of 10:49, 21 February 2008


1ggz, resolution 1.5Å

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CRYSTAL STRUCTURE OF THE CALMODULIN-LIKE PROTEIN (HCLP) FROM HUMAN EPITHELIAL CELLS

Overview

A calmodulin (CaM)-like protein (hCLP) is expressed in human mammary epithelial cells but appears to be limited to certain epithelial cells such as those found in skin, prostate, breast and cervical tissues. A decrease in the expression of this protein is associated with the occurrence of tumors in breast epithelium. The structure of hCLP determined to 1.5 A resolution by X-ray crystallography shows a distinct 30 degrees displacement along the interconnecting central helix, when compared to the highly conserved structure of vertebrate CaM, resulting in a difference in the relative orientation of its two globular domains. Additionally, the electric surface potential landscape at the target protein binding regions on the two globular domains of hCLP is significantly different from those of CaM, indicating that the respective ranges of hCLP and hCaM target proteins do not fully overlap. Observations that hCLP can competitively inhibit CaM activation of target proteins also imply a role for hCLP in which it may also serve as a modulator of CaM activity in the epithelial cells where hCLP is expressed.

About this Structure

1GGZ is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of human calmodulin-like protein: insights into its functional role., Han BG, Han M, Sui H, Yaswen P, Walian PJ, Jap BK, FEBS Lett. 2002 Jun 19;521(1-3):24-30. PMID:12067719

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