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Volumn 342, Issue 6165, 2013, Pages 1477-1483

Crystal structure of a soluble cleaved HIV-1 envelope trimer

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; NEUTRALIZING ANTIBODY; VIRUS GLYCOPROTEIN;

EID: 84890858459     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1245625     Document Type: Article
Times cited : (724)

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    • The complex biantennary glycan observed in the PGT121 paratope in crystal structures (23, 55) is fortuitous, as the glycan comes from a symmetry-related PGT121 Fab molecule in the crystal. Fab PGT121 is glycosylated and was expressed in mammalian cells. PGT121 also reacts on the glycan array with complex biantennary glycans possessing α1-6 sialylated ends (23), which make substantial contacts with the paratope in the crystal structures. Although the N137 glycoform remains uncharacterized on virus-derived HIV-1 Env, PGT121 reactivity with the glycan array, and the liganded crystal structures, suggest that N137 is probably a biantennary complex glycan. The relatively weaker electron density for the oligomannose N137 glycan in the trimer structure also suggests that, when it is not an α1-6 sialylated complex carbohydrate, the N137 glycan lacks major putative sites of interaction with PGT122. Hence, it might not be fully protected from glycosidase treatment, or it may be slightly disordered.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.