1hm6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:03, 21 November 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hm6.gif|left|200px]]
 
-
{{Structure
+
==X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1==
-
|PDB= 1hm6 |SIZE=350|CAPTION= <scene name='initialview01'>1hm6</scene>, resolution 1.80&Aring;
+
<StructureSection load='1hm6' size='340' side='right'caption='[[1hm6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
<table><tr><td colspan='2'>[[1hm6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HM6 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
|GENE= ANX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hm6 OCA], [https://pdbe.org/1hm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hm6 ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hm6 OCA], [http://www.ebi.ac.uk/pdbsum/1hm6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hm6 RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/ANXA1_PIG ANXA1_PIG] Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hm6_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<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/main_output.php?pdb_ID=1hm6 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Annexins comprise a multigene family of Ca2+ and phospholipid- binding proteins. They consist of a conserved C-terminal or core domain that confers Ca2+-dependent phospholipid binding and an N-terminal domain that is variable in sequence and length and responsible for the specific properties of each annexin. Crystal structures of various annexin core domains have revealed a high degree of similarity. From these and other studies it is evident that the core domain harbors the calcium-binding sites that interact with the phospholipid headgroups. However, no structure has been reported of an annexin with a complete N-terminal domain. We have now solved the crystal structure of such a full-length annexin, annexin 1. Annexin 1 is active in membrane aggregation and its refined 1.8 A structure shows an alpha-helical N-terminal domain connected to the core domain by a flexible linker. It is surprising that the two alpha-helices present in the N-terminal domain of 41 residues interact intimately with the core domain, with the amphipathic helix 2-12 of the N-terminal domain replacing helix D of repeat III of the core. In turn, helix D is unwound into a flap now partially covering the N-terminal helix. Implications for membrane aggregation will be discussed and a model of aggregation based on the structure will be presented.
-
'''X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1'''
+
X-ray structure of full-length annexin 1 and implications for membrane aggregation.,Rosengarth A, Gerke V, Luecke H J Mol Biol. 2001 Feb 23;306(3):489-98. PMID:11178908<ref>PMID:11178908</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1hm6" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Annexins comprise a multigene family of Ca2+ and phospholipid- binding proteins. They consist of a conserved C-terminal or core domain that confers Ca2+-dependent phospholipid binding and an N-terminal domain that is variable in sequence and length and responsible for the specific properties of each annexin. Crystal structures of various annexin core domains have revealed a high degree of similarity. From these and other studies it is evident that the core domain harbors the calcium-binding sites that interact with the phospholipid headgroups. However, no structure has been reported of an annexin with a complete N-terminal domain. We have now solved the crystal structure of such a full-length annexin, annexin 1. Annexin 1 is active in membrane aggregation and its refined 1.8 A structure shows an alpha-helical N-terminal domain connected to the core domain by a flexible linker. It is surprising that the two alpha-helices present in the N-terminal domain of 41 residues interact intimately with the core domain, with the amphipathic helix 2-12 of the N-terminal domain replacing helix D of repeat III of the core. In turn, helix D is unwound into a flap now partially covering the N-terminal helix. Implications for membrane aggregation will be discussed and a model of aggregation based on the structure will be presented.
+
*[[Annexin 3D structures|Annexin 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1HM6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM6 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
X-ray structure of full-length annexin 1 and implications for membrane aggregation., Rosengarth A, Gerke V, Luecke H, J Mol Biol. 2001 Feb 23;306(3):489-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11178908 11178908]
+
-
[[Category: Single protein]]
+
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Gerke, V.]]
+
[[Category: Gerke V]]
-
[[Category: Luecke, H.]]
+
[[Category: Luecke H]]
-
[[Category: Rosengarth, A.]]
+
[[Category: Rosengarth A]]
-
[[Category: calcium-free form]]
+
-
[[Category: full-length protein comprising protein core and n-terminal domain]]
+
-
[[Category: phospholipid/ca(2+)-binding protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:31 2008''
+

Current revision

X-RAY STRUCTURE OF FULL-LENGTH ANNEXIN 1

PDB ID 1hm6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hm6"
Personal tools