التفاصيل البيبلوغرافية
العنوان: |
Solution structure of choline binding protein A, the major adhesin of Streptococcus pneumoniae |
المؤلفون: |
Rensheng Luo, Beth Mann, William S Lewis, Arthur Rowe, Richard Heath, Michael L Stewart, Agnes E Hamburger, Siva Sivakolundu, Eilyn R Lacy, Pamela J Bjorkman |
المساهمون: |
The Pennsylvania State University CiteSeerX Archives |
المصدر: |
https://www.ifm.liu.se/edu/coursescms/TFKE37/literature/Strep_EMBOJ_05.pdf. |
سنة النشر: |
2005 |
المجموعة: |
CiteSeerX |
الوصف: |
Streptococcus pneumoniae (pneumococcus) remains a sig-nificant health threat worldwide, especially to the young and old. While some of the biomolecules involved in pneumococcal pathogenesis are known and understood in mechanistic terms, little is known about the molecular details of bacterium/host interactions. We report here the solution structure of the ‘repeated ’ adhesion domains (domains R1 and R2) of the principal pneumococcal adhesin, choline binding protein A (CbpA). Further, we provide insights into the mechanism by which CbpA binds its human receptor, polymeric immunoglobulin receptor (pIgR). The R domains, comprised of 12 imperfect copies of the leucine zipper heptad motif, adopt a unique 3-a-helix, raft-like structure. Each pair of a-helices is antipar-allel and conserved residues in the loop between Helices 1 and 2 exhibit a novel ‘tyrosine fork ’ structure that is involved in binding pIgR. This and other structural fea-tures that we show are conserved in most pneumococcal strains appear to generally play an important role in bacterial adhesion to pIgR. Interestingly, pneumococcus is the only bacterium known to adhere to and invade human cells by binding to pIgR. |
نوع الوثيقة: |
text |
وصف الملف: |
application/pdf |
اللغة: |
English |
Relation: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.579.5461 |
الاتاحة: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.579.5461 |
Rights: |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
رقم الانضمام: |
edsbas.1486463A |
قاعدة البيانات: |
BASE |