THE CALCIUM-BINDING SITES IN HUMAN ANNEXIN-V BY CRYSTAL-STRUCTURE ANALYSIS AT 2.0 A RESOLUTION - IMPLICATIONS FOR MEMBRANE-BINDING AND CALCIUM-CHANNEL ACTIVITY

被引：239

作者：

HUBER, R ^{[1
]}

SCHNEIDER, M ^{[1
]}

MAYR, I ^{[1
]}

ROMISCH, J ^{[1
]}

PAQUES, EP ^{[1
]}

机构：

[1] BEHRINGWERKE AG,FORSCHUNGSLAB,W-3550 MARBURG,GERMANY

来源：

FEBS LETTERS | 1990年 / 275卷 / 1-2期

关键词：

Annexin; Calcium; Channel; Crystal structure; Membrane;

D O I：

10.1016/0014-5793(90)81428-Q

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：

Crystal structure analysis and refinement at 2.0 A resolution of a rhombohedral crystal form of human annexin V at high calcium concentration revealed a domain motion compared to the previously analysed hexagonal crystal form. Five calcium ions were located on the convex face of the molecule. Three strongly bound calciums are liganded at protruding interhelical loops and Asp or Glu residues in homologous positions in repeats I, II and IV. Five proteinaceous oxygens and one solvent molecule form the coordination polyhedron in each case. The unoccupied seventh site is suggested as the phospholipid headgroup binding site. Two more weakly bound sites were identified by lanthanum labelling. The structural features suggest that annexin V attaches with its convex face to membranes by specified calcium mediated interactions with at least three phospholipids. The adjacent membrane bilayer may thus become locally disordered and permeable to allow calcium inflow through the central polar channel of the molecule. © 1990.

引用

页码：15 / 21

页数：7

共 35 条

[1] PROTEIN-KINASE-C INTERACTION WITH CALCIUM - A PHOSPHOLIPID-DEPENDENT PROCESS [J].