1cnp
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1cnp.gif|left|200px]]<br /> | + | [[Image:1cnp.gif|left|200px]]<br /><applet load="1cnp" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1cnp" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1cnp" /> | caption="1cnp" /> | ||
'''THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES'''<br /> | '''THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1CNP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. | + | 1CNP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Known structural/functional Sites: <scene name='pdbsite=LO1:Ion Binding Site'>LO1</scene>, <scene name='pdbsite=LO2:Ion Binding Site'>LO2</scene>, <scene name='pdbsite=LO3:Ion Binding Site'>LO3</scene> and <scene name='pdbsite=LO4:Ion Binding Site'>LO4</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CNP OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 25: | ||
[[Category: s-100 protein]] | [[Category: s-100 protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:39:04 2007'' |
Revision as of 12:29, 18 December 2007
|
THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES
Overview
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.
About this Structure
1CNP is a Single protein structure of sequence from Oryctolagus cuniculus. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Dec 18 14:39:04 2007
