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==THE SOLUTION STRUCTURE OF EGLIN C BASED ON MEASUREMENTS OF MANY NOES AND COUPLING CONSTANTS AND ITS COMPARISON WITH X-RAY STRUCTURES==
==THE SOLUTION STRUCTURE OF EGLIN C BASED ON MEASUREMENTS OF MANY NOES AND COUPLING CONSTANTS AND ITS COMPARISON WITH X-RAY STRUCTURES==
<StructureSection load='1egl' size='340' side='right' caption='[[1egl]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='1egl' size='340' side='right'caption='[[1egl]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1egl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1egl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGL FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6421 Hirudo medicinalis])</td></tr>
</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1egl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egl RCSB], [http://www.ebi.ac.uk/pdbsum/1egl PDBsum]</span></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=1egl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egl OCA], [https://pdbe.org/1egl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egl RCSB], [https://www.ebi.ac.uk/pdbsum/1egl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.  
[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME] Inhibits both elastase and cathepsin G.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egl_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egl_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1egl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A high-precision solution structure of the elastase inhibitor eglin c was determined by NMR and distance geometry calculations. A large set of 947 nuclear Overhauser (NOE) distance constraints was identified, 417 of which were quantified from two-dimensional NOE spectra at short mixing times. In addition, a large number of homonuclear 1H-1H and heteronuclear 1H-15N vicinal coupling constants were used, and constraints on 42 chi 1 and 38 phi angles were obtained. Structure calculations were carried out using the distance geometry program DG-II. These calculations had a high convergence rate, in that 66 out of 75 calculations converged with maximum residual NOE violations ranging from 0.17 A to 0.47 A. The spread of the structures was characterized with average root mean square deviations (&lt;rmsd&gt;) between the structures and a mean structure. To calculate the &lt;rmsd&gt; unbiased toward any single structure, a new procedure was used for structure alignment. A canonical structure was calculated from the mean distances, and all structures were aligned relative to that. Furthermore, an angular order parameter S was defined and used to characterize the spread of structures in torsion angle space. To obtain an accurate estimate of the precision of the structure, the number of calculations was increased until the &lt;rmsd&gt; and the angular order parameters stabilized. This was achieved after approximately 40 calculations. The structure consists of a well-defined core whose backbone deviates from the canonical structure ca. 0.4 A, a disordered N-terminal heptapeptide whose backbone deviates by 0.8-12 A, and a proteinase-binding loop whose backbone deviates up to 3.0 A. Analysis of the angular order parameters and inspection of the structures indicates that a hinge-bending motion of the binding loop may occur in solution. Secondary structures were analyzed by comparison of dihedral angle patterns. The high precision of the structure allows one to identify subtle differences with four crystal structures of eglin c determined in complexes with proteinases.
The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures.,Hyberts SG, Goldberg MS, Havel TF, Wagner G Protein Sci. 1992 Jun;1(6):736-51. PMID:1304915<ref>PMID:1304915</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Eglin|Eglin]]
*[[Eglin|Eglin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
[[Category: Goldberg, M S]]
[[Category: Large Structures]]
[[Category: Havel, T F]]
[[Category: Goldberg MS]]
[[Category: Hyberts, S G]]
[[Category: Havel TF]]
[[Category: Wagner, G]]
[[Category: Hyberts SG]]
[[Category: Proteinase inhibitor]]
[[Category: Wagner G]]

Latest revision as of 13:02, 20 March 2024

THE SOLUTION STRUCTURE OF EGLIN C BASED ON MEASUREMENTS OF MANY NOES AND COUPLING CONSTANTS AND ITS COMPARISON WITH X-RAY STRUCTURESTHE SOLUTION STRUCTURE OF EGLIN C BASED ON MEASUREMENTS OF MANY NOES AND COUPLING CONSTANTS AND ITS COMPARISON WITH X-RAY STRUCTURES

Structural highlights

1egl is a 1 chain structure with sequence from Hirudo medicinalis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ICIC_HIRME Inhibits both elastase and cathepsin G.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

Drag the structure with the mouse to rotate

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OCA
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