METALLOPROTEINS FOR NITRIC OXIDE TRANSPORT AND OTHER ACTIVITIES

用于一氧化氮运输和其他活动的金属蛋白

• 批准号: 7597893
• 负责人: WILLIAM R. MONTFORT
• 金额: $ 0.28万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7597893
• 关键词: Affect; Alpha Particles; Bedbugs; Blood; Carrier Proteins; Complex; Computer Retrieval of Information on Scientific Projects Database; Copper; Freezing; Funding; Grant; Heme; Insecta; Institution; Medical; Metalloproteins; Molecular Chaperones; Nitric Oxide; Organism; Proteins; Research; Research Personnel; Resolution; Resources; Rhodnius; Science; Signaling Molecule; Source; Structure; Synchrotrons; United States National Institutes of Health; interest; mutant; programs; research study; sucking

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This is a program proposal for the study of five nitric oxide (NO) transport proteins called nitrophorins, and for a copper chaperone protein called CueO. NO is a ubiquitous signaling molecule in higher organisms and is of interest to medical and fundamental sciences. The nitrophorins are from two blood-sucking insects, Rhodnius prolixus (rNP1, rNP2, rNP4) and Cimex lectularius (cNP), and provide the best opportunity to date for understanding NO-heme interactions in proteins. We have crystal structures of rNP1, rNP2, and rNP4, and good crystals of cNP and CueO. The proposal is for ultrahigh resolution studies of rNP4 (to 0.8 ¿), structure determinations of NO complexes with all of the nitrophorins and their mutant forms, freeze trapping experiments with NP4, which undergoes a large conformational change in the crystal, and MAD experiments for cNP and CueO. The shorter wavelengths available at the synchrotron are required for the NO complex structure determinations, due to photodissociation or photoreduction affects that occur with Cu K-alpha radiation.

该副本是使用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这是调查员的机构。 这是研究五种称为硝化蛋白的五种一氧化氮（NO）转运蛋白的程序提案，以及一种称为CUEO的铜链酮蛋白。 NO是高等生物中无处不在的信号分子，并且对医学和基础科学感兴趣。亚硝基蛋白来自两种吸血昆虫，Rhodnius prolixus（RNP1，RNP2，RNP4）和Cimex lectularius（CNP），并为了解蛋白质中的无纤维相互作用提供了最好的日期。我们具有RNP1，RNP2和RNP4的晶体结构，以及CNP和CUEO的良好晶体。该提议是针对RNP4的超高分辨率研究（至0.8€），即与所有硝基磷酸蛋白及其突变形式的无配合物的结构测定，使用NP4的冻结诱捕实验，该实验经历了CNP和CUEO的晶体构象变化，并经历了晶体的巨大构象变化。由于光解异位或光换影会影响Cu k-alpha辐射发生的，因此，在同步子上可用的较短波长是无复杂结构确定所必需的。