1kd7
From Proteopedia
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| - | [[Image:1kd7.jpg|left|200px]] | + | [[Image:1kd7.jpg|left|200px]] |
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| - | '''Crystal structure of an extracellular domain fragment of human BAFF''' | + | {{Structure |
| + | |PDB= 1kd7 |SIZE=350|CAPTION= <scene name='initialview01'>1kd7</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of an extracellular domain fragment of human BAFF''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KD7 is a [ | + | 1KD7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KD7 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes., Karpusas M, Cachero TG, Qian F, Boriack-Sjodin A, Mullen C, Strauch K, Hsu YM, Kalled SL, J Mol Biol. 2002 Feb 1;315(5):1145-54. PMID:[http:// | + | Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes., Karpusas M, Cachero TG, Qian F, Boriack-Sjodin A, Mullen C, Strauch K, Hsu YM, Kalled SL, J Mol Biol. 2002 Feb 1;315(5):1145-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11827482 11827482] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tnf]] | [[Category: tnf]] | ||
| - | ''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 12:15:49 2008'' |
Revision as of 10:15, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of an extracellular domain fragment of human BAFF
Overview
B cell activating factor (BAFF), a ligand belonging to the tumor necrosis factor (TNF) family, plays a critical role in regulating survival and activation of peripheral B cell populations and has been associated with autoimmune disease. BAFF is known to interact with three receptors, BCMA, TACI and BAFF-R, that have distant similarities with other receptors of the TNF family. We have determined the crystal structure of the TNF-homologous domain of BAFF at 2.8 A resolution. The structure reveals significant differences when compared to other TNF family members, including an unusually long D-E loop that participates in the formation of a deep, concave and negatively charged region in the putative receptor binding site. The BAFF structure was further used to generate a homology model of APRIL, a closely related TNF family ligand that also binds to BCMA and TACI, but not BAFF-R. Analysis of the putative receptor binding sites of BAFF and APRIL suggests that differences in the D-E loop structure and electrostatic surface potentials may be important for determining binding specificities for BCMA, TACI and BAFF-R.
About this Structure
1KD7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes., Karpusas M, Cachero TG, Qian F, Boriack-Sjodin A, Mullen C, Strauch K, Hsu YM, Kalled SL, J Mol Biol. 2002 Feb 1;315(5):1145-54. PMID:11827482
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