ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Expression, purification, crystallization and preliminary X-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology.Molecular neurobiology · 2009Review
- Optimedin induces expression of N-cadherin and stimulates aggregation of NGF-stimulated PC12 cells.Experimental cell research · 2007Article
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4 authors.
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Abstract
A family of animal proteins is emerging which contain a conserved protein motif known as an olfactomedin (OLF) domain. Novel extracellular protein-protein interactions occur through this domain. The OLF-family member amassin, from the sea urchin Strongylocentrotus purpuratus, has previously been identified to mediate a rapid cell-adhesion event resulting in a large aggregation of coelomocytes, the circulating immune cells. In this work, heterologous expression and purification of the OLF domain from amassin was carried out and initial crystallization trials were performed. A native data set has been collected, extending to 2.7 A under preliminary cryoconditions, using an in-house generator. This work leads the way to the determination of the first structure of an OLF domain.
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