1af3

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[[Image:1af3.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1af3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1af3 OCA], [http://www.ebi.ac.uk/pdbsum/1af3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1af3 RCSB]</span>
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'''RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN'''
'''RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN'''
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[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: Ohta, S.]]
[[Category: Ohta, S.]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: bcl-xl]]
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[[Category: Bcl-xl]]
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[[Category: mitochondrion]]
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[[Category: Mitochondrion]]
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[[Category: regulatory protein]]
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[[Category: Regulatory protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:11:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:39:01 2008''
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Revision as of 07:11, 2 May 2008

Template:STRUCTURE 1af3

RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN


Overview

Bcl-xL is a member of the Bcl-2 protein family, which regulates apoptosis. Preparation of recombinant rat Bcl-xL yielded two forms, one deamidated at -Asn-Gly- sequences to produce isoaspartates and the other not deamidated. The crystal structures of the two forms show that they both adopt an essentially identical backbone structure which resembles the fold of human Bcl-xL: three layers of two alpha-helices each, capped at one end by two short helices. Both forms have a long disordered region, which contains the potential deamidation sites. The molecular structure exhibits a low level of interhelical interactions, the presence of three cavities, and a notable hydrophobic cleft surrounded by walls rich in basic residues. These unique structural features may be favorable for its accommodation into membranes or for possible rearrangement to modulate homo-/heterodimerization. Homology modeling of Bcl-2 and Bax, based on the Bcl-xL structure, suggests that Bax has the strongest potential for membrane insertion. Furthermore, we found a possible interface for interaction with non-Bcl-2 family member proteins, such as CED-4 homologues.

About this Structure

1AF3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family., Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, Morikawa K, J Biol Chem. 1997 Oct 31;272(44):27886-92. PMID:9346936 Page seeded by OCA on Fri May 2 10:11:06 2008

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