Crystal Structure of Rat Bcl-x_L : IMPLICATIONS FOR THE FUNCTION OF THE Bcl-2 PROTEIN FAMILY
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概要
- 論文の詳細を見る
Bcl-x_L is a member of the Bcl-2 protein family, which regulates apoptosis. Preparation of recombinant rat Bcl-x_L 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-x_L : three layers of two α-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, bbased on the Bcl-x_L 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.
- 日本医科大学の論文
- 1998-03-25
著者
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Ohta Shigeo
Department Of Biochemistry And Cell Biology Institute Of Development And Aging Science Graduate Scho
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MORIKAWA Kosuke
Biomolecular Engineering Research Institute
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Inohara Naohiro
Department Of Biochemistry And Cell Biology Institute Of Gerontology Nippon Medical School:(present
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Kunishima Naoki
Biomolecular Engineering Research Institute
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Aritomi Masaharu
Biomolecular Engineering Research Institute
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Ishibashi Yoshitomo
Department of Biochemistry and Cell Biology, Institute of Gerontology, Nippon Medical School
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Ishibashi Yoshitomo
Department Of Biochemistry And Cell Biology Institute Of Gerontology Nippon Medical School
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