1lxl

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(New page: 200px<br /> <applet load="1lxl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxl" /> '''NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PR...)
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<applet load="1lxl" size="450" color="white" frame="true" align="right" spinBox="true"
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'''NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE'''<br />
'''NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE'''<br />
==Overview==
==Overview==
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THE Bcl-2 family of proteins regulate programmed cell death by an unknown, mechanism. Here we describe the crystal and solution structures of a Bcl-2, family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic alpha-helices, which are surrounded by amphipathic, helices. A 60-residue loop connecting helices alpha1 and alpha2 was found, to be flexible and non-essential for anti-apoptotic activity. The three, functionally important Bcl-2 homology regions (BH1, BH2 and BH3) are in, close spatial proximity and form an elongated hydrophobic cleft that may, represent the binding site for other Bcl-2 family members. The arrangement, of the alpha-helices in Bcl-xL is reminiscent of the membrane, translocation domain of bacterial toxins, in particular diphtheria toxin, and the colicins. The structural similarity may provide a clue to the, mechanism of action of the Bcl-2 family of proteins.
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THE Bcl-2 family of proteins regulate programmed cell death by an unknown mechanism. Here we describe the crystal and solution structures of a Bcl-2 family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic alpha-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices alpha1 and alpha2 was found to be flexible and non-essential for anti-apoptotic activity. The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3) are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members. The arrangement of the alpha-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphtheria toxin and the colicins. The structural similarity may provide a clue to the mechanism of action of the Bcl-2 family of proteins.
==About this Structure==
==About this Structure==
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1LXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LXL OCA].
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1LXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXL OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chang, B.S.]]
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[[Category: Chang, B S.]]
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[[Category: Fesik, S.W.]]
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[[Category: Fesik, S W.]]
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[[Category: Harlan, J.E.]]
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[[Category: Harlan, J E.]]
[[Category: Liang, H.]]
[[Category: Liang, H.]]
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[[Category: Meadows, R.P.]]
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[[Category: Meadows, R P.]]
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[[Category: Muchmore, S.W.]]
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[[Category: Muchmore, S W.]]
[[Category: Nettesheim, D.]]
[[Category: Nettesheim, D.]]
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[[Category: Ng, S.C.]]
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[[Category: Ng, S C.]]
[[Category: Sattler, M.]]
[[Category: Sattler, M.]]
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[[Category: Thompson, C.B.]]
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[[Category: Thompson, C B.]]
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[[Category: Wong, S.L.]]
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[[Category: Wong, S L.]]
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[[Category: Yoon, H.S.]]
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[[Category: Yoon, H S.]]
[[Category: apoptosis]]
[[Category: apoptosis]]
[[Category: bcl-2 family]]
[[Category: bcl-2 family]]
[[Category: programmed cell death]]
[[Category: programmed cell death]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:05:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:24 2008''

Revision as of 11:49, 21 February 2008


1lxl

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NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH, MINIMIZED AVERAGE STRUCTURE

Overview

THE Bcl-2 family of proteins regulate programmed cell death by an unknown mechanism. Here we describe the crystal and solution structures of a Bcl-2 family member, Bcl-xL (ref. 2). The structures consist of two central, primarily hydrophobic alpha-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices alpha1 and alpha2 was found to be flexible and non-essential for anti-apoptotic activity. The three functionally important Bcl-2 homology regions (BH1, BH2 and BH3) are in close spatial proximity and form an elongated hydrophobic cleft that may represent the binding site for other Bcl-2 family members. The arrangement of the alpha-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphtheria toxin and the colicins. The structural similarity may provide a clue to the mechanism of action of the Bcl-2 family of proteins.

About this Structure

1LXL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death., Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW, Nature. 1996 May 23;381(6580):335-41. PMID:8692274

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