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1cdu

From Proteopedia

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[[Image:1cdu.gif|left|200px]]<br />
 
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<applet load="1cdu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cdu, resolution 2.7&Aring;" />
 
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'''STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 MUTANT WITH PHE 43 REPLACED BY VAL'''<br />
 
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==Overview==
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==STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 MUTANT WITH PHE 43 REPLACED BY VAL==
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The T-cell antigen coreceptor CD4 also serves as the receptor for the, envelope glycoprotein gp120 of HIV. Extensive mutational analysis of CD4, has implicated residues from a portion of the extracellular amino-terminal, domain (D1) in gp120 binding. However, none of these proteins has been, fully characterized biophysically, and thus the precise effects on, molecular structure and binding interactions are unknown. In the present, study, we produced soluble versions of three mutant CD4 molecules (F43V, G47S, and A55F) and characterized their structural properties, thermostability, and ability to bind gp120. Crystallographic and, thermodynamic analysis showed minimal structural alterations in the F43V, and G47S mutant proteins, which have solvent-exposed mutant side chains., In contrast, some degree of disorder appears to exist in the folded state, of A55F, as a result of mutating a buried side chain. Real time kinetic, measurements of the interaction of the mutant proteins with gp120 showed, affinity decreases of 5-fold for G47S, 50-fold for A55F, and 200-fold for, F43V. Although both rate constants for the binding reaction were affected, by these mutations, the loss in affinity was mainly due to a decrease in, on rates, with less drastic changes occurring in the off rates. These, observations suggest the involvement of conformational adaptation in the, CD4-gp120 interaction. Together, the structural and kinetic data confirm, that F43V is a critical residue in gp120 recognition site, which may also, include main chain interactions at residue Gly-47.
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<StructureSection load='1cdu' size='340' side='right'caption='[[1cdu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cdu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CDU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cdu OCA], [https://pdbe.org/1cdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cdu RCSB], [https://www.ebi.ac.uk/pdbsum/1cdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cdu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CD4_HUMAN CD4_HUMAN] Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cd/1cdu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1cdu ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CDU 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=1CDU OCA].
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*[[CD4 3D structures|CD4 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding., Wu H, Myszka DG, Tendian SW, Brouillette CG, Sweet RW, Chaiken IM, Hendrickson WA, Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15030-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8986758 8986758]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brouillette, C.G.]]
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[[Category: Brouillette CG]]
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[[Category: Chaiken, I.M.]]
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[[Category: Chaiken IM]]
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[[Category: Hendrickson, W.A.]]
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[[Category: Hendrickson WA]]
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[[Category: Myszka, D.]]
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[[Category: Myszka D]]
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[[Category: Sweet, R.W.]]
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[[Category: Sweet RW]]
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[[Category: Tendian, S.W.]]
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[[Category: Tendian SW]]
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[[Category: Wu, H.]]
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[[Category: Wu H]]
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[[Category: glycoprotein]]
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[[Category: immunoglobulin fold]]
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[[Category: lipoprotein]]
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[[Category: mhc]]
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[[Category: t-cell]]
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[[Category: t-cell surface glycoprotein]]
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[[Category: transmembrane]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:20:44 2007''
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Current revision

STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 MUTANT WITH PHE 43 REPLACED BY VAL

PDB ID 1cdu

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