The crystal structure of a high oxygen affinity species of haemoglobin   (bar-headed goose haemoglobin in the oxy form)

doi:10.1006/jmbi.1996.0040

CORC > 北京大学 > 生命科学学院

	The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)
	Zhang, J ; Hua, ZQ ; Tame, JRH ; Lu, GY ; Zhang, RJ ; Gu, XC
刊名	分子生物学杂志
	1996
关键词	crystallography haemoglobin high-altitude adaptation HIGH-ALTITUDE HEMOGLOBIN MECHANISM STEREOCHEMISTRY RESPIRATION ADAPTATION REFINEMENT RESOLUTION OXIDATION BINDING
DOI	10.1006/jmbi.1996.0040
英文摘要	We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 Angstrom. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood shows a greatly elevated oxygen affinity compared to closely related species of geese. This is apparently due to a single proline to alanine mutation at the alpha(1) beta(1) interface which destabilises the T state of the protein. The beta chain N and C termini are well-localized, and together with other neighbouring basic groups they form a strongly positively charged groove at the entrance to the central cavity around the molecular dyad. The well-ordered conformation and the three-dimensional distribution of positive charges clearly indicate this area to be the inositol pentaphosphate binding site of bird haemoglobins. (C) 1996 Academic Press Limited; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:A1996TQ24200014&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; SCI(E); PubMed; 60; ARTICLE; 3; 484-493; 255
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/202050]
专题	生命科学学院
推荐引用方式 GB/T 7714	Zhang, J,Hua, ZQ,Tame, JRH,et al. The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)[J]. 分子生物学杂志,1996.
APA	Zhang, J,Hua, ZQ,Tame, JRH,Lu, GY,Zhang, RJ,&Gu, XC.(1996).The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form).分子生物学杂志.
MLA	Zhang, J,et al."The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)".分子生物学杂志 (1996).