1c28
From Proteopedia
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| - | [[Image:1c28.gif|left|200px]] | + | [[Image:1c28.gif|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR''' | + | {{Structure |
| + | |PDB= 1c28 |SIZE=350|CAPTION= <scene name='initialview01'>1c28</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C28 is a [ | + | 1C28 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C28 OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor., Shapiro L, Scherer PE, Curr Biol. 1998 Mar 12;8(6):335-8. PMID:[http:// | + | The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor., Shapiro L, Scherer PE, Curr Biol. 1998 Mar 12;8(6):335-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9512423 9512423] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: acrp30 c1q tnf trimer all-beta]] | [[Category: acrp30 c1q tnf trimer all-beta]] | ||
| - | ''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 10:18:54 2008'' |
Revision as of 08:18, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR
Overview
ACRP30--adipocyte complement-related protein of 30 kDa or AdipoQ--is an abundant serum protein, secreted exclusively from fat cells, which is implicated in energy homeostasis and obesity [1,2]. ACRP30 is a close homologue of the complement protein C1q, which is involved in the recognition of microbial surfaces [3-5] and antibody-antigen complexes [6,7] in the classical pathway of complement. We have determined the crystal structure of a homotrimeric fragment from ACRP30 at 2.1 A resolution. The structure reveals an unexpected homology to the tumor necrosis factor (TNF) family. Identical folding topologies, key residue conservations, and similarity of trimer interfaces and intron positions firmly establish an evolutionary link between the TNF and C1q families. We suggest that TNFs--which control many aspects of inflammation, adaptive immunity, apoptosis and energy homeostasis--arose by divergence from a primordial recognition molecule of the innate immune system. The evolutionary connection between C1q-like proteins and TNFs illuminates the shared functions of these two important groups of proteins.
About this Structure
1C28 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor., Shapiro L, Scherer PE, Curr Biol. 1998 Mar 12;8(6):335-8. PMID:9512423
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