1MAZ

X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED CELL DEATH

Summary for 1MAZ

• Entry DOI: 10.2210/pdb1maz/pdb
• Related: 1bxl
• Descriptor: Bcl-2-like protein 1 (2 entities in total)
• Functional Keywords: apoptosis, programmed cell death, bcl-2 family
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion membrane; Single-pass membrane protein (By similarity): Q07817
• Total number of polymer chains: 1
• Total formula weight: 24879.37

Authors

Muchmore, S.W.,Sattler, M.,Liang, H.,Meadows, R.P.,Harlan, J.E.,Yoon, H.S.,Nettesheim, D.,Chang, B.S.,Thompson, C.B.,Wong, S.L.,Ng, S.C.,Fesik, S.W. (deposition date: 1996-04-09, release date: 1997-04-21, Last modification date: 2024-02-14)

Primary citation

Muchmore, S.W.,Sattler, M.,Liang, H.,Meadows, R.P.,Harlan, J.E.,Yoon, H.S.,Nettesheim, D.,Chang, B.S.,Thompson, C.B.,Wong, S.L.,Ng, S.L.,Fesik, S.W.
X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.
Nature, 381:335-341, 1996

PubMed Abstract: 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.

PubMed: 8692274
DOI: 10.1038/381335a0

Experimental method

X-RAY DIFFRACTION (2.2 Å)