Rhodocetin

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Rhodocetin heterotetramer subunit α (grey), β (green), γ (pink), δ (yellow) (PDB code 3gpr)

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Updated on 07-May-2020

1sb2 - MpvRtn subunits αβ - Malayan pit viper
3gpr - MpvRtn subunits αβγδ
6nde, 6ndd, 6ndf, 6ndh, 6nda, 6ndc, 6ndb, 6nd8, 6ndg, 6nd9, 5thp - MpvRtn subunits γδ + integrin α-2 + ion

↑ Wang R, Kini RM, Chung MC. Rhodocetin, a novel platelet aggregation inhibitor from the venom of Calloselasma rhodostoma (Malayan pit viper): synergistic and noncovalent interaction between its subunits. Biochemistry. 1999 Jun 8;38(23):7584-93. PMID:10360956 doi:http://dx.doi.org/10.1021/bi982132z
↑ Niland S, Komljenovic D, Macas J, Bracht T, Bauerle T, Liebner S, Eble JA. Rhodocetin-alphabeta selectively breaks the endothelial barrier of the tumor vasculature in HT1080 fibrosarcoma and A431 epidermoid carcinoma tumor models. Oncotarget. 2018 Apr 27;9(32):22406-22422. doi: 10.18632/oncotarget.25032., eCollection 2018 Apr 27. PMID:29854288 doi:http://dx.doi.org/10.18632/oncotarget.25032
↑ Eble JA, Niland S, Bracht T, Mormann M, Peter-Katalinic J, Pohlentz G, Stetefeld J. The alpha2beta1 integrin-specific antagonist rhodocetin is a cruciform, heterotetrameric molecule. FASEB J. 2009 Sep;23(9):2917-27. Epub 2009 Apr 15. PMID:19369383 doi:10.1096/fj.08-126763

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 == Structural highlights ==
-Rhodocetin 3D structure shows a tetramer of distinct homologous subunits α,β,γ and δ.  The quaternary structure is distinct from that of snake venom CLPs.  The γ,δ subunits are responsible for tn binding to integrin α-2 domain<ref>PMID:19369383</ref>.
+Rhodocetin 3D structure shows a <scene name='84/842889/Xc/2'>tetramer of distinct homologous subunits α,β,γ and δ</scene>. The quaternary structure is distinct from that of snake venom CLPs. The γ,δ subunits are responsible for tn binding to integrin α-2 domain<ref>PMID:19369383</ref>.
 </StructureSection>