6T3O

Crystal structure of the human myomesin domain 10

Summary for 6T3O

• Entry DOI: 10.2210/pdb6t3o/pdb
• Descriptor: Myomesin-1, AZIDE ION (3 entities in total)
• Functional Keywords: small protein domain, scaffold structure, contractile protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 15437.46

Authors

Duskova, J.,Petrokova, H.,Maly, P. (deposition date: 2019-10-11, release date: 2021-03-17, Last modification date: 2024-01-24)

Primary citation

Kuchar, M.,Kosztyu, P.,Daniel Liskova, V.,Cerny, J.,Petrokova, H.,Vroblova, E.,Maly, M.,Vankova, L.,Krupka, M.,Raskova Kafkova, L.,Turanek Knotigova, P.,Duskova, J.,Dohnalek, J.,Masek, J.,Turanek, J.,Raska, M.,Maly, P.
Myomedin scaffold variants targeted to 10E8 HIV-1 broadly neutralizing antibody mimic gp41 epitope and elicit HIV-1 virus-neutralizing sera in mice.
Virulence, 12:1271-1287, 2021

PubMed Abstract: One of the proposed strategies for the development of a more efficient HIV-1 vaccine is based on the identification of proteins binding to a paratope of chosen broadly neutralizing antibody (bNAb) that will mimic cognate HIV-1 Env (glyco)protein epitope and could be used as potent immunogens for induction of protective virus-neutralizing antibodies in the immunized individuals. To verify this "non-cognate ligand" concept, we developed a highly complex combinatorial library designed on a scaffold of human myomesin-1 protein domain and selected proteins called Myomedins specifically binding to variable regions of HIV-1 broadly neutralizing antibody 10E8. Immunization of mice with these Myomedin variants elicited the production of HIV-1 Env-specific antibodies. Hyperimmune sera bound to Env pseudotyped viruses and weakly/moderately neutralized 54% of tested clade A, B, C, and AE pseudotyped viruses variants . These results demonstrate that Myomedin variants have the potential to mimic Env epitopes and could be used as potential HIV-1 vaccine components.

PubMed: 33993840
DOI: 10.1080/21505594.2021.1920251

Experimental method

X-RAY DIFFRACTION (1.8 Å)