1RZG
Crystal structure of Human anti-HIV-1 GP120 reactive antibody 412d
Summary for 1RZG
Entry DOI | 10.2210/pdb1rzg/pdb |
Related | 1RZ7 1RZ8 1RZF 1RZI 1RZJ 1RZK |
Related PRD ID | PRD_900003 |
Descriptor | Fab 412d light chain, Fab 412d heavy chain, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, ... (6 entities in total) |
Functional Keywords | hiv-1; gp120; cd4i; antibodies; tyrosine sulfation; vh-gene usage, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 99135.71 |
Authors | Huang, C.C.,Venturi, M.,Majeed, S.,Moore, M.J.,Phogat, S.,Zhang, M.-Y.,Dimitrov, D.S.,Hendrickson, W.A.,Robinson, J.,Sodroski, J.,Wyatt, R.,Choe, H.,Farzan, M.,Kwong, P.D. (deposition date: 2003-12-24, release date: 2004-02-03, Last modification date: 2024-11-06) |
Primary citation | Huang, C.C.,Venturi, M.,Majeed, S.,Moore, M.J.,Phogat, S.,Zhang, M.-Y.,Dimitrov, D.S.,Hendrickson, W.A.,Robinson, J.,Sodroski, J.,Wyatt, R.,Choe, H.,Farzan, M.,Kwong, P.D. Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120 Proc.Natl.Acad.Sci.USA, 101:2706-2711, 2004 Cited by PubMed Abstract: The conserved surface of the HIV-1 gp120 envelope glycoprotein that binds to the HIV-1 coreceptor is protected from humoral recognition by multiple layers of camouflage. Here we present sequence and genomic analyses for 12 antibodies that pierce these defenses and determine the crystal structures of 5. The data reveal mechanisms and atomic-level details for three unusual immune features: posttranslational mimicry of coreceptor by tyrosine sulfation of antibody, an alternative molecular mechanism controlling such sulfation, and highly selective V(H)-gene usage. When confronted by extraordinary viral defenses, the immune system unveils novel adaptive capabilities, with tyrosine sulfation enhancing the vocabulary of antigen recognition. PubMed: 14981267DOI: 10.1073/pnas.0308527100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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