| Literature DB >> 15644210 |
Stéphane Réty1, Jana Sopková-de Oliveira Santos, Lise Dreyfuss, Karine Blondeau, Katerina Hofbauerová, Céline Raguénès-Nicol, Daniel Kerboeuf, Madalena Renouard, Françoise Russo-Marie, Anita Lewit-Bentley.
Abstract
Annexin A8 is a relatively infrequent and poorly studied member of this large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia. We have solved its three-dimensional structure, which includes a moderately long and intact N terminus. The structure is closest to that of annexin A3 and highlights several important regions of inherent flexibility in the annexin molecule. The N terminus resembles that of annexin A3, as it lies along the concave surface of the molecule and inserts partially into the hydrophilic channel in its centre. Since both annexins A3 and A8 are expressed in promyelocytic cells during their differentiation, the similarity in their structures might suggest a functional relationship.Entities:
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Year: 2004 PMID: 15644210 DOI: 10.1016/j.jmb.2004.11.015
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469