Cephalopod Hemocyanins: Structure and Function

头足类血蓝蛋白：结构和功能

• 批准号: 9805570
• 负责人: Karen Miller
• 金额: $ 33万
• 依托单位: Oregon State University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-09-01 至 2003-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9805570&HistoricalAwards=false
• 关键词: Cephalopod; Hemocyanins; Structure; Function

The study focuses on the structure and physiological function of hemocyanins, which are oxygen-carrying proteins found in the blood of some invertebrates. The amino acid sequence, and part of the 3-dimensional structure of one of these giant molecules (that from Octopus) has recently been determined by the investigator and her collaborators. The new work proposed will first examine the structure of a part of the gene for the Octopus hemocyanin, and then attempt to develop a system to express a portion of this gene in bacteria or other cells. This should ultimately allow directed mutation, to analyze the effects of particular amino acids on the oxygen binding function. The protein also contains attached carbohydrate groups; the composition and structure of representative ones will be determined, and their possible roles in determining protein structure and/or function examined. Finally, the program will focus on how portions of these giant molecules communicate with one another to regulate the cooperative binding of oxygen on many sites. This phenomenon of allosteric regulation is common to many other important proteins, and is still not completely understood.Hemocyanins are oxygen transport proteins found exclusively in molluscs and arthropods. The octopus hemocyanins are truly enormous molecules, with molecular weights in the millions. As a result of recent breakthroughs in structure and sequence analysis of these molecules, the investigators are poised to interpret the evolution and function of hemocyanin at a level of sophistication never before possible.

该研究的重点是血胶蛋白的结构和生理功能，这些结构和生理功能是在某些无脊椎动物的血液中发现的含氧蛋白。 氨基酸序列以及这些巨型分子之一（来自章鱼）的三维结构的一部分，最近由研究者及其合作者确定。 提出的新工作将首先检查章鱼血氰蛋白基因的一部分的结构，然后尝试开发一个系统以在细菌或其他细胞中表达该基因的一部分。 这最终应允许定向突变，分析特定氨基酸对氧结合功能的影响。 该蛋白质还含有附着的碳水化合物基团；将确定代表性的组成和结构，及其在确定蛋白质结构和/或功能中的可能作用。 最后，该程序将重点介绍这些巨型分子的一部分如何相互通信，以调节氧对许多地点的合作结合。 变构调节的这种现象对于许多其他重要蛋白质都是共同的，并且仍然没有完全理解。-氨基糖蛋白是仅在软体动物和节肢动物中发现的氧气转运蛋白。 章鱼血红蛋白是真正的巨大分子，数百万分子量。 由于最近对这些分子的结构和序列分析进行突破的结果，研究者有望在以前从未做出的成熟水平上解释血氰蛋白酶的演变和功能。