ATPase-ATPase Interactions in Sarcoplasmic Reticulum
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Martin Poe', 'PO_EMAI': None, 'PO_PHON': None}
The structure of the Ca2+-ATPase of sarcoplasmic reticulum will                 be analyzed by crystallographic and spectroscopic techniques.                   One aim of the work will be to produce three-dimensional crystals               of the Ca2+ transport ATPase in appropriate size and stability                  for high resolution X-ray diffraction analysis.  In addition,                   reconstruction of the structure of Ca2+-ATPase by electron                      microscopy of the E1 and E2type two-dimensional Ca2+-ATPase                     crystals will be refined and the structural differences between                 the E1 and the E2 conformations identified.  The information                    obtained will be correlated with kinetic data to develop a                      molecular description of the Ca transport process.                                                                                                              The complete molecular machinery required for the ATP-dependent                 translocation of Ca2+ from the cytoplasm into the lumen of                      sarcoplasmic reticulum is contained in the Ca2+ transport ATPase.                                                                                               The Ca2+-ATPase is present in different iso-forms in the                        sarcoplasmic reticulum of slow or fast skeletal, cardiac and                    smooth muscles.  These data will fill an important gap in our                   knowledge of the structure of sarcoplasmic reticulum and will                   significantly contribute to the elucidation of the molecular                    mechanism of calcium transport.
{'FirstName': 'Anthony', 'LastName': 'Martonosi', 'PI_MID_INIT': 'N', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Anthony N Martonosi', 'EmailAddress': '3154734701', 'NSF_ID': '000103531', 'StartDate': '06/21/1993', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'SUNY, Upstate Medical University', 'CityName': 'SYRACUSE', 'ZipCode': '132102306', 'PhoneNumber': '3154645476', 'StreetAddress': '750 E ADAMS ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'New York', 'StateCode': 'NY', 'CONGRESSDISTRICT': '22', 'CONGRESS_DISTRICT_ORG': 'NY22', 'ORG_UEI_NUM': 'HYN3WD58HNN7', 'ORG_LGL_BUS_NAME': 'RESEARCH FOUNDATION FOR THE STATE UNIVERSITY OF NEW YORK, THE', 'ORG_PRNT_UEI_NUM': 'GMZUKXFDJMA9'}
{'Name': 'SUNY, Upstate Medical University', 'CityName': 'SYRACUSE', 'StateCode': 'NY', 'ZipCode': '132102306', 'StreetAddress': '750 E ADAMS ST', 'CountryCode': 'US', 'CountryName': 'United States', 'StateName': 'New York', 'CountryFlag': '1', 'CONGRESSDISTRICT': '22', 'CONGRESS_DISTRICT_PERF': 'NY22'}
[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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