2b1u: Difference between revisions

(13 intermediate revisions by the same user not shown)

Line 1:

~~[[Image:2b1u.gif|left|200px]]<br />~~

~~<applet load="2b1u" size="450" color="white" frame="true" align="right" spinBox="true"~~

~~caption="2b1u" />~~

~~'''Solution structure of Calmodulin-like Skin Protein C terminal domain'''<br />~~

==~~Overview~~==

==Solution structure of Calmodulin-like Skin Protein C terminal domain==

The structure and dynamics of human calmodulin-like skin protein (CLSP), have been characterized by NMR spectroscopy. The mobility of CLSP has been, found to be different for the N-terminal and C-terminal domains. The, isolated domains were also expressed and analyzed. The structure of the, isolated C-terminal domain is presented. The N-terminal domain is, characterized by four stable helices, which experience large fluctuations., This is shown to be due to mutations in the hydrophobic core. The overall, N-terminal domain behavior is similar both in the full-length protein and, in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP, to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By, using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties, were investigated. Finally, CLSP is framed into the evolutionary scheme of, the calmodulin-like family.

== Structural highlights ==

<table><tr><td colspan='2'>[[2b1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B1U FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1u OCA], [https://pdbe.org/2b1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b1u RCSB], [https://www.ebi.ac.uk/pdbsum/2b1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1u ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/CALL5_HUMAN CALL5_HUMAN] Binds calcium. May be involved in terminal differentiation of keratinocytes.

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b1/2b1u_consurf.spt"</scriptWhenChecked>

<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2b1u ConSurf].

== Publication Abstract from PubMed ==

The structure and dynamics of human calmodulin-like skin protein (CLSP) have been characterized by NMR spectroscopy. The mobility of CLSP has been found to be different for the N-terminal and C-terminal domains. The isolated domains were also expressed and analyzed. The structure of the isolated C-terminal domain is presented. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties were investigated. Finally, CLSP is framed into the evolutionary scheme of the calmodulin-like family.

~~==About this~~ Structure==

A structural and dynamic characterization of the EF-hand protein CLSP.,Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C Structure. 2006 Jun;14(6):1029-38. PMID:16765896<ref>PMID:16765896</ref>

~~2B1U is a [http~~:~~//en.wikipedia~~.~~org/wiki/Single_protein Single protein] structure of sequence from [http~~:~~//en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http~~:/~~/ispc.weizmann.ac.il/oca-bin/ocashort?id=2B1U OCA].~~

~~==Reference==~~

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

~~A structural and dynamic characterization~~ of the ~~EF-hand protein CLSP~~.~~, Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C, Structure~~. ~~2006 Jun;14(6):1029~~-~~38. PMID:[http~~://~~ispc.weizmann.ac.il~~/~~/pmbin/getpm?pmid=16765896 16765896]~~

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: ~~Single protein~~]]

[[Category: Large Structures]]

[[Category: Babini, E.]]

[[Category: Babini E]]

[[Category: Bertini, I.]]

[[Category: Bertini I]]

[[Category: Capozzi, F.]]

[[Category: Capozzi F]]

[[Category: Chirivino, E.]]

[[Category: Chirivino E]]

[[Category: Luchinat, C.]]

[[Category: Luchinat C]]

~~[[Category: SPINE, Structural.Proteomics.in.Europe.]]~~

~~[[Category: backbone dynamic]]~~

~~[[Category: calmodulin-like skin protein]]~~

~~[[Category: clsp]]~~

~~[[Category: nmr]]~~

~~[[Category: solution structure]]~~

~~[[Category: spine]]~~

~~[[Category: structural genomics]]~~

~~[[Category: structural proteomics in europe]]~~

~~''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:57:10 2007''~~

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:2b1u.gif|left|200px]]<br />
-<applet load="2b1u" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2b1u" />
-'''Solution structure of Calmodulin-like Skin Protein C terminal domain'''<br />
-==Overview==
+==Solution structure of Calmodulin-like Skin Protein C terminal domain==
-The structure and dynamics of human calmodulin-like skin protein (CLSP), have been characterized by NMR spectroscopy. The mobility of CLSP has been, found to be different for the N-terminal and C-terminal domains. The, isolated domains were also expressed and analyzed. The structure of the, isolated C-terminal domain is presented. The N-terminal domain is, characterized by four stable helices, which experience large fluctuations., This is shown to be due to mutations in the hydrophobic core. The overall, N-terminal domain behavior is similar both in the full-length protein and, in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP, to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By, using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties, were investigated. Finally, CLSP is framed into the evolutionary scheme of, the calmodulin-like family.
+<StructureSection load='2b1u' size='340' side='right'caption='[[2b1u]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2b1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B1U FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1u OCA], [https://pdbe.org/2b1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b1u RCSB], [https://www.ebi.ac.uk/pdbsum/2b1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1u ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CALL5_HUMAN CALL5_HUMAN] Binds calcium. May be involved in terminal differentiation of keratinocytes.
+== 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/b1/2b1u_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2b1u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structure and dynamics of human calmodulin-like skin protein (CLSP) have been characterized by NMR spectroscopy. The mobility of CLSP has been found to be different for the N-terminal and C-terminal domains. The isolated domains were also expressed and analyzed. The structure of the isolated C-terminal domain is presented. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties were investigated. Finally, CLSP is framed into the evolutionary scheme of the calmodulin-like family.
-==About this Structure==
+A structural and dynamic characterization of the EF-hand protein CLSP.,Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C Structure. 2006 Jun;14(6):1029-38. PMID:16765896<ref>PMID:16765896</ref>
-B1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B1U OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-A structural and dynamic characterization of the EF-hand protein CLSP., Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C, Structure. 2006 Jun;14(6):1029-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16765896 16765896]
+</div>
+<div class="pdbe-citations 2b1u" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Babini, E.]]
+[[Category: Babini E]]
-[[Category: Bertini, I.]]
+[[Category: Bertini I]]
-[[Category: Capozzi, F.]]
+[[Category: Capozzi F]]
-[[Category: Chirivino, E.]]
+[[Category: Chirivino E]]
-[[Category: Luchinat, C.]]
+[[Category: Luchinat C]]
-[[Category: SPINE, Structural.Proteomics.in.Europe.]]
-[[Category: backbone dynamic]]
-[[Category: calmodulin-like skin protein]]
-[[Category: clsp]]
-[[Category: nmr]]
-[[Category: solution structure]]
-[[Category: spine]]
-[[Category: structural genomics]]
-[[Category: structural proteomics in europe]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:57:10 2007''