Venezuelan Institute for Scientific Research (IVIC) in Caracas, Venezuela, where he started his scientifc career as visiting student in 1966. After his postdoctoral work at the MRC Laboratory of Molecular Biology (Cambridge, UK) with Hugh E. Huxley, he founded the Deparment of Structural Biology of IVIC in 1997, where he was an International Research Scholar of the Howard Hughes Medical Institute (HHMI) from 1997 until 2011. He has devoted his career to the study of the structure and function of the myosin thick filaments of skeletal, cardiac and smooth muscle and the myosin interacting-head motif (IHM) structure and function, with their implications on the muscle relaxed state, super-relaxation, thick filament activation and human muscle diseases like hypertrophic and dilated cardiomyopathy. His honors includes: Premio FEP "Lorenzo Mendoza Fleury" ("Lorenzo Mendoza Fleury" Prize) (1991) of Fundación Empresas Polar (FEP); CONICIT Biology Prizes (1989, 1990, 1996); FONACIT Biology Prize (2005); and the National Prize in Science and Technology of Venezuela (2008). He is a member of the Latin-American Academy of Sciences (ACAL) and The World Academy of Sciences (TWAS).
|Center of Structural
Biology (CBE) "Humberto Fernández-Morán"
CBE is a node of the Centro de Biología Estructural del Mercosur (CeBEM), houses the Centro Latino-Américano FEI de Crio-Microscopía Electrónica (CLAFCME) and was founded in honor of Humberto Fernández-Morán, the cryo-EM pioneer.
Read (in Spanish) how the Center of Structural Biology "Humberto Fernández-Morán was created
The CBE and CLAFCME web pages can only be seen on IVIC´s intranet: Centro de Biología Esttuctural (CBE) , Centro Latino-Américano FEI de Crio-Microscopía Electrónica (CLAFCME)
Contact information: Centro de Biología Estructural "Humberto Fernández-Morán", IVIC, APDO 20632, Caracas 1020A, Venezuela. Phone:+58-212-504-1435 (sec) Twitter: @raulpadron E-mail: Clases
Retired Research Associates (working ad honorem): Electronic Eng. Antonio Pinto EE, Lic. Biology Lorenzo Alamo
Research associates: Dr. Gustavo Márquez, M. Sc. Ruth García, M. Sc. Galax Joya. Eng. Franklin Méndez
Undergraduated students: Br. Sebastián Duno
Associated Investigators: Dr. Guidenn Sulbarán (20-2-2016, France)
Former research Associates: Dr. Jose Reinaldo Guerrero (Retired), M. Sc. Maristela Granados, Eng. Franklin Méndez (back on 18-9-2017), Dr. Aivett Bilbao (U.S.A.)
Postdoctoral Fellows: Dr. Carlos Hidalgo 1997-2000 (Now in U.S.A.), Dr. Rosalba Rodriguez 2009-2012 (Now at IVIC-CBE), Dr. Guidenn Sulbáran 2009-2012 (France 20-2-2016), Dr. Lucía Proietti d´Speratti (Now in U.S.A. 1-2-2016)
Ph. D Graduates: Dr. Jose Reinaldo Guerrero 1995, Dr. Julio Ortiz 2002 (Now in France), Dr. María Elena Zoghbi 2003 (Now in U.S.A.), Dr. Reicy Brito 2010 (Now in Spain).
M. Sc. Graduates,: Dr. Nelly Panté 1986 (Now in Canada), Dr. José Reinaldo Guerrero 1989, M. Sc. Maristela Granados 1993, M. Sc. Karina Temperini 2001 (Now in Argentina), M. Sc. Nelitza Linarez 2001, Dr. Antonio Biasutto 2011- (Now in U.K.).
Lic. Biology graduates: Dr.Hernando Sosa 1986 (Now in U.S.A.), Lic. Patricia Valero 1991, Lic. Jackeline Rodriguez 1991
B. Sc. Graduates: Dr. Claire L. Riggs 2010 (Now in U.S.A.)
Lab visitors. Dr.Robert Perz-Edwards 1991-1992 (Now in U.S.A.), Leroy Lindsay MD 2005 (Now in Spain), Mina-Han Tran 2008/2009 (Now in U.S.A.)
Academic tree Tree
lab latest publications
|Padron lab four questions
2 nm resolution three-dimensional reconstruction of tarantula striated muscle thick filament
|Quasi-atomic model of the tarantula thick
filament and the tarantula IHM PDB 3JBH quasi-atomic model
|Myosin II Interacting-Heads Motif (IHM) quasi-atomic models|
Tarantula myosin II and paramyosin sequences
|How the relaxed thik filament structure is conserved?|
|How the relaxed IHM structure is conserved?|
thick filaments and IHMs are relaxed and activated?
|How thick filaments malfunction on disease?|
|IHM implications on hypertrophic (HCM) and dilated (DCM) cardiomyopathy|
myosin variants on interacting-heads motif (IHM) explain
distinct hypertrophic (HCM) and dilated (DCM) cardiomyopathy phenotypes
Lorenzo Alamo, James S. Ware, Antonio Pinto, Richard E. Gillilan, Jonathan G. Seidman, Christine E. Seidman & Raúl Padrón eLife 2017;6:e24634 doi: 10.7554/eLife.24634
Cardiac β-myosin variants cause hypertrophic cardiomyopathy (HCM) or dilated cardiomyopathy (DCM) by disrupting sarcomere contraction and relaxation. The locations of variants on isolated myosin head structures predict contractility effects but not the prominent relaxation and energetic deficits that characterize HCM. During relaxation, pairs of myosins form interacting-heads motif (IHM) structures that with other sarcomere proteins establish an energy-saving, super-relaxed (SRX) state. Using a human β-cardiac myosin IHM quasi-atomic model (PDB 5TBY), we defined interactions sites between adjacent myosin heads and associated protein partners, and then analyzed rare variants from 6112 HCM and 1315 DCM patients and 33,370 ExAC controls. HCM variants, 72% that changed electrostatic charges, disproportionately altered IHM interaction residues (expected 23%; HCM 54%, p=2.6×10−19; DCM 26%, p=0.66; controls 20%, p=0.23). HCM variant locations predict impaired IHM formation and stability, and attenuation of the SRX state - accounting for altered contractrility, reduced diastolic relaxation, and increased energy consumption, that fully characterize HCM pathogenesis.
lab journal covers