This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4x9p

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 18:35, 1 February 2017

Crystal structure of bovine Annexin A2

Structural highlights

4x9p is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ANXA2_BOVIN] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity.

Publication Abstract from PubMed

The progression of aggressive cancer occurs via angiogenesis and metastasis making these processes important targets for the development of anti-cancer agents. However, recent studies have raised the concern that selective inhibition of angiogenesis results in a switch towards increased tumour growth and metastasis. Since Annexin A2 (AnxA2) is involved in both angiogenesis and metastasis, it may serve as an ideal target for the simultaneous inhibition of both processes. Based on the discovery that domains I (DI) and IV (DIV) of AnxA2 are potent inhibitors of angiogenesis, we designed seven peptides derived from these domains based on AnxA2 crystal structures. The peptides were expressed as fusion peptides to increase their folding and solubility. Light scattering, far-UV circular dichroism and thermal transition analyses were employed to investigate their aggregation tendencies, alpha-helical propensity and stability, respectively. 2,2,2-trifluoroethanol (50%) increased the alpha-helical propensities of all peptides, indicating that they may favour a hydrophobic environment, but did not enhance their thermal stability. DI-P2 appears to be the most stable and folded peptide in a hydrophilic environment. The secondary structure of DI-P2 was confirmed by nuclear magnetic resonance spectra. The effect of the seven AnxA2 peptides on the formation and integrity of capillary-like networks was studied in a co-culture system mimicking many of the angiogenesis-related processes. Notably, DI-P2 inhibited significantly network formation in this system, indicating that the folded DI-P2 peptide interferes with vascular endothelial growth factor-dependent pro-angiogenic processes. Thus, this peptide has the potential of being developed further as an anti-angiogenic drug.

The Native Structure of Annexin A2 Peptides in Hydrophilic Environment Determines their Anti-Angiogenic Effects.,Raddum AM, Hollas H, Shumilin I, Henklein P, Kretsinger R, Fossen T, Vedeler A Biochem Pharmacol. 2015 Mar 12. pii: S0006-2952(15)00132-X. doi:, 10.1016/j.bcp.2015.02.013. PMID:25772737^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Raddum AM, Hollas H, Shumilin I, Henklein P, Kretsinger R, Fossen T, Vedeler A. The Native Structure of Annexin A2 Peptides in Hydrophilic Environment Determines their Anti-Angiogenic Effects. Biochem Pharmacol. 2015 Mar 12. pii: S0006-2952(15)00132-X. doi:, 10.1016/j.bcp.2015.02.013. PMID:25772737 doi:http://dx.doi.org/10.1016/j.bcp.2015.02.013

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4x9p"

@@ Line 1: / Line 1: @@
 ==Crystal structure of bovine Annexin A2==
 <StructureSection load='4x9p' size='340' side='right' caption='[[4x9p]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4x9p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X9P FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x9p RCSB], [http://www.ebi.ac.uk/pdbsum/4x9p PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9p OCA], [http://pdbe.org/4x9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x9p RCSB], [http://www.ebi.ac.uk/pdbsum/4x9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9p ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4x9p" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Annexin|Annexin]]
 == References ==
 <references/>

4x9p

From Proteopedia

Revision as of 18:35, 1 February 2017

Crystal structure of bovine Annexin A2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox