2cdx | pdb_00002cdx
STRUCTURE OF COBRA CARDIOTOXIN CTXI AS DERIVED FROM NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DISTANCE GEOMETRY CALCULATIONS
Structural highlights
Function[3SA1_NAJAT] Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities on many other cells, including red blood cells. Interaction with sulfatides in the cell membrane induces pore formation and cell internalization and is responsible for cytotoxicity in cardiomyocytes. It targets the mitochondrial membrane and induces mitochondrial swelling and fragmentation (By similarity). It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity and inhibits protein kinases C (PubMed:8448165). It also binds with high affinity to heparin (PubMed:17685633). It also causes skeletal muscle necrosis after intramuscular injection into mice (PubMed:8342169).[UniProtKB:P60301][1] [2] 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 PubMedThe structure of cardiotoxin CTX I from Naja naja atra has been investigated by NMR spectroscopy. Sequence specific resonance assignments have been obtained for all backbone protons as well as for most side-chain protons. Distance geometry calculations were carried out using a metric matrix DG program. A total of 715 NOE constraints, 27 phi angle constraints and a list of the hydrogen bond donors were used for the metric matrix DG calculations and refinement. The average pairwise r.m.s.d. of the resulting structures was 1.01 A for the backbone heavy atoms, and 1.69 A for all heavy atoms. The protein is rich in beta structure and consists of a large triple-stranded, antiparallel beta sheet as well as a short double-stranded, antiparallel beta sheet. Non-regular hydrogen bonding is found between side-chains of the carboxy-terminal end and the rest of the core region. The structure is discussed in terms of evolutionary aspects as well as recent investigations about the biological function and active site. Structure of cobra cardiotoxin CTX I as derived from nuclear magnetic resonance spectroscopy and distance geometry calculations.,Jahnke W, Mierke DF, Beress L, Kessler H J Mol Biol. 1994 Jul 29;240(5):445-58. PMID:8046750[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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