1cnp

From Proteopedia

(Difference between revisions)

Revision as of 10:44, 19 May 2021

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

Structural highlights

1cnp is a 2 chain structure with sequence from Oryctolagus cuniculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[S10A6_RABIT] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).

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 S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.

The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.,Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ Nat Struct Biol. 1995 Sep;2(9):790-6. PMID:7552751^[1]

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

References

↑ Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ. The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins. Nat Struct Biol. 1995 Sep;2(9):790-6. PMID:7552751

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/1cnp"

@@ Line 3: / Line 3: @@
 <StructureSection load='1cnp' size='340' side='right'caption='[[1cnp]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cnp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CNP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cnp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNP FirstGlance]. <br>
-</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=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [http://pdbe.org/1cnp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB], [http://www.ebi.ac.uk/pdbsum/1cnp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnp ProSAT]</span></td></tr>
+</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=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [https://pdbe.org/1cnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB], [https://www.ebi.ac.uk/pdbsum/1cnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
+[[https://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[S100 protein|S100 protein]]
+*[[S100 proteins 3D structures|S100 proteins 3D structures]]
 == References ==
 <references/>

1cnp

From Proteopedia

Revision as of 10:44, 19 May 2021

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

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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