1bxl: Difference between revisions

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New page: left|200px<br /> <applet load="1bxl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxl" /> '''STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NM...
 
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[[Image:1bxl.gif|left|200px]]<br />
[[Image:1bxl.gif|left|200px]]<br /><applet load="1bxl" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1bxl" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1bxl" />
caption="1bxl" />
'''STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
'''STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />


==Overview==
==Overview==
Heterodimerization between members of the Bcl-2 family of proteins is a, key event in the regulation of programmed cell death. The molecular basis, for heterodimer formation was investigated by determination of the, solution structure of a complex between the survival protein Bcl-xL and, the death-promoting region of the Bcl-2-related protein Bak. The structure, and binding affinities of mutant Bak peptides indicate that the Bak, peptide adopts an amphipathic alpha helix that interacts with Bcl-xL, through hydrophobic and electrostatic interactions. Mutations in, full-length Bak that disrupt either type of interaction inhibit the, ability of Bak to heterodimerize with Bcl-xL.
Heterodimerization between members of the Bcl-2 family of proteins is a key event in the regulation of programmed cell death. The molecular basis for heterodimer formation was investigated by determination of the solution structure of a complex between the survival protein Bcl-xL and the death-promoting region of the Bcl-2-related protein Bak. The structure and binding affinities of mutant Bak peptides indicate that the Bak peptide adopts an amphipathic alpha helix that interacts with Bcl-xL through hydrophobic and electrostatic interactions. Mutations in full-length Bak that disrupt either type of interaction inhibit the ability of Bak to heterodimerize with Bcl-xL.


==About this Structure==
==About this Structure==
1BXL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1BXL OCA].  
1BXL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1BXL OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Chang, B.S.]]
[[Category: Chang, B S.]]
[[Category: Eberstadt, M.]]
[[Category: Eberstadt, M.]]
[[Category: Fesik, S.W.]]
[[Category: Fesik, S W.]]
[[Category: Harlan, J.E.]]
[[Category: Harlan, J E.]]
[[Category: Liang, H.]]
[[Category: Liang, H.]]
[[Category: Meadows, R.P.]]
[[Category: Meadows, R P.]]
[[Category: Minn, A.J.]]
[[Category: Minn, A J.]]
[[Category: Nettesheim, D.]]
[[Category: Nettesheim, D.]]
[[Category: Sattler, M.]]
[[Category: Sattler, M.]]
[[Category: Shuker, S.B.]]
[[Category: Shuker, S B.]]
[[Category: Thompson, C.B.]]
[[Category: Thompson, C B.]]
[[Category: Yoon, H.]]
[[Category: Yoon, H.]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
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[[Category: complex (apoptosis/peptide)]]
[[Category: complex (apoptosis/peptide)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:15:14 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:09 2008''