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3cd4
From Proteopedia
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| - | [[Image:3cd4.jpg|left|200px]]<br /><applet load="3cd4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="3cd4, resolution 2.2Å" /> | ||
| - | '''REFINEMENT AND ANALYSIS OF THE FIRST TWO DOMAINS OF HUMAN CD4'''<br /> | ||
| - | == | + | ==REFINEMENT AND ANALYSIS OF THE FIRST TWO DOMAINS OF HUMAN CD4== |
| + | <StructureSection load='3cd4' size='340' side='right'caption='[[3cd4]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3cd4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cd4 2cd4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CD4 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]] 2.2Å</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=3cd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cd4 OCA], [https://pdbe.org/3cd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3cd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cd4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| + | == 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/cd/3cd4_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=3cd4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The structure of a fragment of human CD4 containing two immunoglobulin (Ig)-like domains has been determined by X-ray crystallography and refined at 2.2 A resolution. The structure determination involved iterative building and simulated-annealing refinement, beginning with a partial model. Comparison of domain 1 with an Ig variable domain shows that CD4 has a long and prominent CDR2-like loop (the C"C" corner) and shortened CC' and FG loops (which mediate dimerization in IgV modules). Comparison of domain 2 with Ig modules and domain 1 shows that it can be described as a truncated Ig V domain, in which strands C" and D are deleted. The intersheet disulfide in domain 2 is absent, and there is an altered packing of the two beta-sheets together with a remodeling of the hydrophobic core. The interface between domains 1 and 2 is a lap joint with an extensive hydrophobic surface. The key features of domain 1 that contribute to the interface are found at corresponding positions in domain 2, leading us to propose that the contact between domains 2 and 3 will resemble the one between domains 1 and 2. | The structure of a fragment of human CD4 containing two immunoglobulin (Ig)-like domains has been determined by X-ray crystallography and refined at 2.2 A resolution. The structure determination involved iterative building and simulated-annealing refinement, beginning with a partial model. Comparison of domain 1 with an Ig variable domain shows that CD4 has a long and prominent CDR2-like loop (the C"C" corner) and shortened CC' and FG loops (which mediate dimerization in IgV modules). Comparison of domain 2 with Ig modules and domain 1 shows that it can be described as a truncated Ig V domain, in which strands C" and D are deleted. The intersheet disulfide in domain 2 is absent, and there is an altered packing of the two beta-sheets together with a remodeling of the hydrophobic core. The interface between domains 1 and 2 is a lap joint with an extensive hydrophobic surface. The key features of domain 1 that contribute to the interface are found at corresponding positions in domain 2, leading us to propose that the contact between domains 2 and 3 will resemble the one between domains 1 and 2. | ||
| - | + | Refinement and analysis of the structure of the first two domains of human CD4.,Garrett TP, Wang J, Yan Y, Liu J, Harrison SC J Mol Biol. 1993 Dec 5;234(3):763-78. PMID:8254672<ref>PMID:8254672</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 3cd4" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[CD4 3D structures|CD4 3D structures]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Garrett | + | [[Category: Garrett TPJ]] |
| - | [[Category: Harrison | + | [[Category: Harrison SC]] |
| - | [[Category: Wang | + | [[Category: Wang J]] |
| - | [[Category: Yan | + | [[Category: Yan Y]] |
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Current revision
REFINEMENT AND ANALYSIS OF THE FIRST TWO DOMAINS OF HUMAN CD4
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