1af3
From Proteopedia
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| - | [[Image:1af3.gif|left|200px]] | + | [[Image:1af3.gif|left|200px]] |
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| - | '''RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN''' | + | {{Structure |
| + | |PDB= 1af3 |SIZE=350|CAPTION= <scene name='initialview01'>1af3</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RAT BCL-XL AN APOPTOSIS INHIBITORY PROTEIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AF3 is a [ | + | 1AF3 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9346936 9346936] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: regulatory protein]] | [[Category: regulatory protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:56:42 2008'' |
Revision as of 07:56, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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