1w3w

From Proteopedia

(Difference between revisions)

Revision as of 05:57, 8 February 2016

THE 2.1 ANGSTROEM RESOLUTION STRUCTURE OF ANNEXIN A8

Structural highlights

1w3w is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1w45
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w3w"

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     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w3w ConSurf].
 <div style="clear:both"></div>
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1w3w

From Proteopedia

Revision as of 05:57, 8 February 2016

THE 2.1 ANGSTROEM RESOLUTION STRUCTURE OF ANNEXIN A8

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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