3cd4
From Proteopedia
(New page: 200px<br /> <applet load="3cd4" size="450" color="white" frame="true" align="right" spinBox="true" caption="3cd4, resolution 2.2Å" /> '''REFINEMENT AND ANALY...) |
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caption="3cd4, resolution 2.2Å" /> | 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'''<br /> | ||
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==Overview== | ==Overview== | ||
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. | ||
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: CD4 lymphocyte deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186940 186940]], Lupus erythematosus, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=186940 186940]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 3CD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 2CD4. Full crystallographic information is available from [http:// | + | 3CD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 2CD4. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CD4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: t-cell surface glycoprotein]] | [[Category: t-cell surface glycoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:43:04 2008'' |
Revision as of 15:43, 15 February 2008
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REFINEMENT AND ANALYSIS OF THE FIRST TWO DOMAINS OF HUMAN CD4
Contents |
Overview
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.
Disease
Known diseases associated with this structure: CD4 lymphocyte deficiency OMIM:[186940], Lupus erythematosus, susceptibility to OMIM:[186940]
About this Structure
3CD4 is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 2CD4. Full crystallographic information is available from OCA.
Reference
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
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