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| | <StructureSection load='3cd4' size='340' side='right'caption='[[3cd4]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3cd4' size='340' side='right'caption='[[3cd4]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3cd4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=3CD4 FirstGlance]. <br> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3cd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cd4 OCA], [http://pdbe.org/3cd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3cd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cd4 ProSAT]</span></td></tr> | + | </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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Garrett, T P.J]] | + | [[Category: Garrett TPJ]] |
| - | [[Category: Harrison, S C]] | + | [[Category: Harrison SC]] |
| - | [[Category: Wang, J]] | + | [[Category: Wang J]] |
| - | [[Category: Yan, Y]] | + | [[Category: Yan Y]] |
| - | [[Category: T-cell surface glycoprotein]]
| + | |
| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Garrett TP, Wang J, Yan Y, Liu J, Harrison SC. Refinement and analysis of the structure of the first two domains of human CD4. J Mol Biol. 1993 Dec 5;234(3):763-78. PMID:8254672 doi:http://dx.doi.org/10.1006/jmbi.1993.1625
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