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Q33819243-B158E6F6-EA9E-4F52-A1DA-3B14C196F8FF
Q33819243-B158E6F6-EA9E-4F52-A1DA-3B14C196F8FF
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http://www.wikidata.org/entity/statement/Q33819243-B158E6F6-EA9E-4F52-A1DA-3B14C196F8FF
The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.
P2860
Q33819243-B158E6F6-EA9E-4F52-A1DA-3B14C196F8FF
BestRank
Statement
http://www.wikidata.org/entity/statement/Q33819243-B158E6F6-EA9E-4F52-A1DA-3B14C196F8FF
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wasDerivedFrom
6c2948e55c89ea015df5a7deed75c03989d198f4
P2860
Homolog-scanning mutagenesis reveals poliovirus receptor residues important for virus binding and replication.