1af3
From Proteopedia
(New page: 200px<br /><applet load="1af3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1af3, resolution 2.5Å" /> '''RAT BCL-XL AN APOPTOS...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1af3.gif|left|200px]]<br /><applet load="1af3" size=" | + | [[Image:1af3.gif|left|200px]]<br /><applet load="1af3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1af3, resolution 2.5Å" /> | caption="1af3, resolution 2.5Å" /> | ||
'''RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN'''<br /> | '''RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bcl-xL is a member of the Bcl-2 protein family, which regulates apoptosis. | + | 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== | ==About this Structure== | ||
| - | 1AF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1AF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AF3 OCA]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: regulatory protein]] | [[Category: regulatory protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:52 2008'' |
Revision as of 09:43, 21 February 2008
|
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 Thu Feb 21 11:43:52 2008
