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1bt6

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P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN II N-TERMINUS

Structural highlights

1bt6 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

S10AA_HUMAN Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.

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

The aggregation and membrane fusion properties of annexin II are modulated by the association with a regulatory light chain called p11.p11 is a member of the S100 EF-hand protein family, which is unique in having lost its calcium-binding properties. We report the first structure of a complex between p11 and its cognate peptide, the N-terminus of annexin II, as well as that of p11 alone. The basic unit for p11 is a tight, non-covalent dimer. In the complex, each annexin II peptide forms hydrophobic interactions with both p11 monomers, thus providing a structural basis for high affinity interactions between an S100 protein and its target sequence. Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.

The crystal structure of a complex of p11 with the annexin II N-terminal peptide.,Rety S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A Nat Struct Biol. 1999 Jan;6(1):89-95. PMID:9886297^[1]

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

References

↑ Rety S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A. The crystal structure of a complex of p11 with the annexin II N-terminal peptide. Nat Struct Biol. 1999 Jan;6(1):89-95. PMID:9886297 doi:10.1038/4965

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/1bt6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bt6' size='340' side='right'caption='[[1bt6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bt6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BT6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bt6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BT6 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bt6 OCA], [https://pdbe.org/1bt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bt6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/S10AA_HUMAN S10AA_HUMAN]] Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase. [[https://www.uniprot.org/uniprot/ANXA2_CHICK ANXA2_CHICK]] Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity.
+[https://www.uniprot.org/uniprot/S10AA_HUMAN S10AA_HUMAN] Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Gerke, V]]
+[[Category: Gerke V]]
-[[Category: Lewit-Bentley, A]]
+[[Category: Lewit-Bentley A]]
-[[Category: Osterloh, D]]
+[[Category: Osterloh D]]
-[[Category: Renouard, M]]
+[[Category: Renouard M]]
-[[Category: Rety, S]]
+[[Category: Rety S]]
-[[Category: Russo-Marie, F]]
+[[Category: Russo-Marie F]]
-[[Category: Sopkova, J]]
+[[Category: Sopkova J]]
-[[Category: Calcium/phospholipid binding protein]]
-[[Category: Ef-hand protein]]
-[[Category: Ligand of annexin ii]]
-[[Category: S100 family]]

1bt6

From Proteopedia

Current revision

P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN II N-TERMINUS

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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