| Structural highlights
2zzo is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | NonStd Res: | |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The S138A substitution of fusion inhibitory peptides derived from the C-terminal heptad repeat (C-HR) of the human immunodeficiency virus type 1 (HIV-1) gp41 leads to enhanced binding affinity to the N-terminal heptad repeat (N-HR). As such, these peptides exhibit highly potent anti-HIV-1 activity. X-ray crystallographic analysis was performed to understand the effect of the substitution on binding affinity. The comparison of the native and S138A crystal structures indicated that the increase in the hydrophobicity of the S138A substitution may aid the stabilization of the N-HR/C-HR complex through additional hydrophobic contacts. Free-energy calculations suggest that the difference between the desolvation free energies of the C-HR-derived peptides with and without the S138A mutation dominates the observed difference in anti-HIV-1 activity.
X-ray crystallographic study of an HIV-1 fusion inhibitor with the gp41 S138A substitution.,Watabe T, Terakawa Y, Watanabe K, Ohno H, Nakano H, Nakatsu T, Kato H, Izumi K, Kodama E, Matsuoka M, Kitaura K, Oishi S, Fujii N J Mol Biol. 2009 Sep 25;392(3):657-65. Epub 2009 Jul 17. PMID:19616557[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Watabe T, Terakawa Y, Watanabe K, Ohno H, Nakano H, Nakatsu T, Kato H, Izumi K, Kodama E, Matsuoka M, Kitaura K, Oishi S, Fujii N. X-ray crystallographic study of an HIV-1 fusion inhibitor with the gp41 S138A substitution. J Mol Biol. 2009 Sep 25;392(3):657-65. Epub 2009 Jul 17. PMID:19616557 doi:10.1016/j.jmb.2009.07.027
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