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| | {{STRUCTURE_1hqv| PDB=1hqv | SCENE= }} | | {{STRUCTURE_1hqv| PDB=1hqv | SCENE= }} |
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| - | '''STRUCTURE OF APOPTOSIS-LINKED PROTEIN ALG-2'''
| + | ===STRUCTURE OF APOPTOSIS-LINKED PROTEIN ALG-2=== |
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| - | ==Overview==
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| - | BACKGROUND: The Ca2+ binding apoptosis-linked gene-2 (ALG-2) protein acts as a proapoptotic factor in a variety of cell lines and is required either downstream or independently of caspases for apoptosis to occur. ALG-2 belongs to the penta-EF-hand (PEF) protein family and has two high-affinity and one low-affinity Ca2+ binding sites. Like other PEF proteins, its N terminus contains a Gly/Pro-rich segment. Ca2+ binding is required for the interaction with the target protein, ALG-2 interacting protein 1 (AIP1). RESULTS: We present the 2.3 A resolution crystal structure of Ca2+-Ioaded des1-20ALG-2 (aa 21-191), which was obtained by limited proteolysis of recombinant ALG-2 with elastase. The molecule contains eight alpha helices that fold into five EF-hands, and, similar to other members of this protein family, the molecule forms dimers. Ca2+ ions bind to EF1, EF3, and, surprisingly, to EF5. In the related proteins calpain and grancalcin, the EF5 does not bind Ca2+ and is thought to primarily facilitate dimerization. Most importantly, the conformation of des1-20ALG-2 is significantly different from that of calpain and grancalcin. This difference can be described as a rigid body rotation of EF1-2 relative to EF4-5 and the dimer interface, with a hinge within the EF3 loop. An electron density, which is interpreted as a hydrophobic Gly/Pro-rich decapeptide that is possibly derived from the cleaved N terminus, was found in a hydrophobic cleft between these two halves of the molecule. CONCLUSIONS: A different relative orientation of the N- and C-terminal halves of des1-20ALG-2 in the presence of Ca2+ and the peptide as compared to other Ca2+loaded PEF proteins changes substantially the shape of the molecule, exposing a hydrophobic patch on the surface for peptide binding and a large cleft near the dimer interface. We postulate that the binding of a Gly/ Pro-rich peptide in the presence of Ca2+ induces a conformational rearrangement in ALG-2, and that this mechanism is common to other PEF proteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11525164}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11525164 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11525164}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Calcium binding protein]] | | [[Category: Calcium binding protein]] |
| | [[Category: Penta-ef-hand protein]] | | [[Category: Penta-ef-hand protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:08:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:33:33 2008'' |
Revision as of 05:33, 1 July 2008
Template:STRUCTURE 1hqv
STRUCTURE OF APOPTOSIS-LINKED PROTEIN ALG-2
Template:ABSTRACT PUBMED 11525164
About this Structure
1HQV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of apoptosis-linked protein ALG-2: insights into Ca2+-induced changes in penta-EF-hand proteins., Jia J, Tarabykina S, Hansen C, Berchtold M, Cygler M, Structure. 2001 Apr 4;9(4):267-75. PMID:11525164
Page seeded by OCA on Tue Jul 1 08:33:33 2008
