Structural highlights
Function
ANXA8_HUMAN This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The crystal structure of annexin A8 is similar to that of annexin A3.,Rety S, Sopkova-de Oliveira Santos J, Dreyfuss L, Blondeau K, Hofbauerova K, Raguenes-Nicol C, Kerboeuf D, Renouard M, Russo-Marie F, Lewit-Bentley A J Mol Biol. 2005 Feb 4;345(5):1131-9. Epub 2004 Dec 8. PMID:15644210[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rety S, Sopkova-de Oliveira Santos J, Dreyfuss L, Blondeau K, Hofbauerova K, Raguenes-Nicol C, Kerboeuf D, Renouard M, Russo-Marie F, Lewit-Bentley A. The crystal structure of annexin A8 is similar to that of annexin A3. J Mol Biol. 2005 Feb 4;345(5):1131-9. Epub 2004 Dec 8. PMID:15644210 doi:10.1016/j.jmb.2004.11.015
