Phylogenetic analysis and homology modelling of Paracentrotus lividus nectin
Molecular Diversity, ISSN: 1381-1991, Vol: 14, Issue: 4, Page: 653-665
2010
- 22Citations
- 21Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations22
- Citation Indexes22
- 22
- CrossRef18
- Captures21
- Readers21
- 21
Article Description
The extracellular matrix protein Pl-nectin, a 210-kDa homodimer originally purified from sea urchin eggs, plays a crucial role in cell adhesion and embryonic morphogenesis. The compiled cDNA sequence, obtained by RT-PCR primer walking and 3′ RACE, identified a 984aa product containing a 23aa signal peptide and including all six internal peptides identified by protein microsequencing. The protein is a new member of the galactose-binding protein superfamily as it consists of six 151-156aa-long tandemly repeated domains (D1-D6), homologous to the discoidin-like domains, also known as F5/8-type C domains. Based on homology modelling, we present a three-dimensional structure (3D) for D5, identified as the prototype domain. The molecular modelling of the assembled Pl-nectin homodimer accounts for a Pl-nectin quaternary structure composed of two 105-kDa C-shaped monomers linked by a S-S bridge. The presence of an LDT motif between the first and the second exposed loops of the D2 domain suggests the binding of Pl-nectin to an integrin receptor. Altogether, the in silico analysis described here is consistent with previous biochemical reports and offers a basis for predictions to be experimentally tested. © 2009 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=78650169840&origin=inward; http://dx.doi.org/10.1007/s11030-009-9203-3; http://www.ncbi.nlm.nih.gov/pubmed/19908157; http://link.springer.com/10.1007/s11030-009-9203-3; http://www.springerlink.com/index/10.1007/s11030-009-9203-3; http://www.springerlink.com/index/pdf/10.1007/s11030-009-9203-3; https://dx.doi.org/10.1007/s11030-009-9203-3; https://link.springer.com/article/10.1007/s11030-009-9203-3
Springer Science and Business Media LLC
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