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[[Image:1ic5.jpg|left|200px]]<br /><applet load="1ic5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ic5, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD99A)-HEN LYSOZYME COMPLEX'''<br />


==Overview==
==CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD99A)-HEN LYSOZYME COMPLEX==
A structural and thermodynamic study of the entropic contribution of salt, bridge formation to the interaction between hen egg white lysozyme (HEL), and the variable domain fragment (Fv) of anti-HEL antibody, HyHEL-10, was, carried out. Three Fv mutants (HD32A, HD96A, and HD32AD96A) were prepared, and the interactions between the mutant Fvs and HEL were investigated., Crystallography revealed that the overall structures of these mutant, complexes were almost identical to that of wild-type Fv. Little structural, changes were observed in the HD32AD96A mutant-HEL complex, and two water, molecules were introduced into the mutation site, indicating that the two, water molecules structurally compensated for the complete removal of the, salt bridges. This result suggests that the entropic contribution of the, salt bridge originates from dehydration. In the singly mutated complexes, one water molecule was also introduced into the mutated site, bridging the, antigen-antibody interface. However, a local structural difference was, observed in the HD32A Fv-HEL complex, and conformational changes occurred, due to changes in the relative orientation of the heavy chain to the light, chain upon complexation in HD96A Fv-HEL complexes. The reduced affinity of, these single mutants for the antigen originates from the increase in, entropy loss, indicating that these structural changes also introduced an, increase in entropy loss. These results suggest that salt bridge formation, makes an entropic contribution to the protein antigen-antibody interaction, through reduction of entropy loss due to dehydration and structural, changes.
<StructureSection load='1ic5' size='340' side='right'caption='[[1ic5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ic5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IC5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=1ic5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ic5 OCA], [https://pdbe.org/1ic5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ic5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ic5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ic5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KV5A9_MOUSE KV5A9_MOUSE]
== 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/ic/1ic5_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=1ic5 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IC5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IC5 OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
==Reference==
__TOC__
Structural evidence for entropic contribution of salt bridge formation to a protein antigen-antibody interaction: the case of hen lysozyme-HyHEL-10 Fv complex., Shiroishi M, Yokota A, Tsumoto K, Kondo H, Nishimiya Y, Horii K, Matsushima M, Ogasahara K, Yutani K, Kumagai I, J Biol Chem. 2001 Jun 22;276(25):23042-50. Epub 2001 Apr 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11297547 11297547]
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Horii K]]
[[Category: Horii, K.]]
[[Category: Kondo H]]
[[Category: Kondo, H.]]
[[Category: Kumagai I]]
[[Category: Kumagai, I.]]
[[Category: Matsushima M]]
[[Category: Matsushima, M.]]
[[Category: Nishimiya Y]]
[[Category: Nishimiya, Y.]]
[[Category: Ogasahara K]]
[[Category: Ogasahara, K.]]
[[Category: Shiroishi M]]
[[Category: Shiroishi, M.]]
[[Category: Tsumoto K]]
[[Category: Tsumoto, K.]]
[[Category: Yokota A]]
[[Category: Yokota, A.]]
[[Category: Yutani K]]
[[Category: Yutani, K.]]
[[Category: anti-hen egg white lysozyme antibody]]
[[Category: antigen-antibody complex]]
[[Category: hyhel-10]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:00:48 2008''

Latest revision as of 10:46, 3 April 2024

CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD99A)-HEN LYSOZYME COMPLEXCRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD99A)-HEN LYSOZYME COMPLEX

Structural highlights

1ic5 is a 3 chain structure with sequence from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KV5A9_MOUSE

Evolutionary Conservation

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

See Also

1ic5, resolution 2.30Å

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