1aey: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1aey" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aey" /> '''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTI...
 
OCA (talk | contribs)
No edit summary
 
(19 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1aey.gif|left|200px]]<br /><applet load="1aey" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1aey" />
'''ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES'''<br />


==Overview==
==ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, SOLUTION NMR, 15 STRUCTURES==
The assignment of the 1H and 15N nuclear magnetic resonance spectra of the, Src-homology region 3 domain of chicken brain alpha-spectrin has been, obtained. A set of solution structures has been determined from distance, and dihedral angle restraints, which provide a reasonable representation, of the protein structure in solution, as evaluated by a principal, component analysis of the global pairwise root-mean-square deviation, (rmsd) in a large set of structures consisting of the refined and, unrefined solution structures and the crystal structure. The solution, structure is well defined, with a lower degree of convergence between the, structures in the loop regions than in the secondary structure elements., The average pairwise rmsd between the 15 refined solution structures is, 0.71 +/- 0.13 A for the backbone atoms and 1.43 +/- 0.14 A for all heavy, atoms. The solution structure is basically the same as the crystal, structure. The average rmsd between the 15 refined solution structures and, the crystal structure is 0.76 A for the backbone atoms and 1.45 +/- 0.09 A, for all heavy atoms. There are, however, small differences probably caused, by intermolecular contacts in the crystal structure.
<StructureSection load='1aey' size='340' side='right'caption='[[1aey]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aey]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AEY 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=1aey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aey OCA], [https://pdbe.org/1aey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aey RCSB], [https://www.ebi.ac.uk/pdbsum/1aey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aey ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPTN1_CHICK SPTN1_CHICK] Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
== 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/ae/1aey_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=1aey ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The assignment of the 1H and 15N nuclear magnetic resonance spectra of the Src-homology region 3 domain of chicken brain alpha-spectrin has been obtained. A set of solution structures has been determined from distance and dihedral angle restraints, which provide a reasonable representation of the protein structure in solution, as evaluated by a principal component analysis of the global pairwise root-mean-square deviation (rmsd) in a large set of structures consisting of the refined and unrefined solution structures and the crystal structure. The solution structure is well defined, with a lower degree of convergence between the structures in the loop regions than in the secondary structure elements. The average pairwise rmsd between the 15 refined solution structures is 0.71 +/- 0.13 A for the backbone atoms and 1.43 +/- 0.14 A for all heavy atoms. The solution structure is basically the same as the crystal structure. The average rmsd between the 15 refined solution structures and the crystal structure is 0.76 A for the backbone atoms and 1.45 +/- 0.09 A for all heavy atoms. There are, however, small differences probably caused by intermolecular contacts in the crystal structure.


==About this Structure==
1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure.,Blanco FJ, Ortiz AR, Serrano L J Biomol NMR. 1997 Jun;9(4):347-57. PMID:9255941<ref>PMID:9255941</ref>
1AEY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AEY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure., Blanco FJ, Ortiz AR, Serrano L, J Biomol NMR. 1997 Jun;9(4):347-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9255941 9255941]
</div>
<div class="pdbe-citations 1aey" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Spectrin 3D structures|Spectrin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Blanco, F.J.]]
[[Category: Blanco FJ]]
[[Category: Ortiz, A.R.]]
[[Category: Ortiz AR]]
[[Category: Serrano, L.]]
[[Category: Serrano L]]
[[Category: calcium-binding]]
[[Category: capping protein]]
[[Category: cytoskeleton]]
[[Category: duplication]]
[[Category: repeat]]
[[Category: sh3 domain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:48:11 2007''