The atomic structure of human methemalbumin at 1.9 Å

被引：310

作者：

Wardell, M ^{[1
]}

Wang, ZM ^{[1
]}

Ho, JX ^{[1
]}

Robert, J ^{[1
]}

Ruker, F ^{[1
]}

Ruble, J ^{[1
]}

Carter, DC ^{[1
]}

机构：

[1] New Century Pharmaceut Inc, Huntsville, AL 35824 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 291卷 / 04期

基金：

美国国家航空航天局;

关键词：

hemalbumin; crystal structure; blood substitutes;

D O I：

10.1006/bbrc.2002.6540

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 Angstrom. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 Angstrom) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented. (C) 2002 Elsevier Science (USA).

引用

页码：813 / 819

页数：7

共 35 条

[1] HEME-PEPTIDE PROTEIN INTERACTIONS - THE BINDING OF HEME OCTAPEPTIDES AND UNDECAPEPTIDES, AND MICROPEROXIDASE-8 AND MICROPEROXIDASE-11, TO HUMAN-SERUM ALBUMIN [J].