1ain

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spinqualitylabelsall models 1ain, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION

Overview

cDNA coding for N-terminally truncated human annexin I, a member of the, family of Ca(2+)-dependent phospholipid binding proteins, has been cloned, and expressed in Escherichia coli. The expressed protein is biologically, active, and has been purified and crystallized in space group, P2(1)2(1)2(1) with cell dimensions a = 139.36 A, b = 67.50 A, and c =, 42.11 A. The crystal structure has been determined by molecular, replacement at 3.0 A resolution using the annexin V core structure as the, search model. The average backbone deviation between these two structures, is 2.34 A. The structure has been refined to an R-factor of 17.7% at 2.5 A, resolution. Six calcium sites have been identified in the annexin I, structure. Each is located in the loop region of the helix-loop-helix, motif. Two of the six calcium sites in annexin I are not occupied in the, annexin V structure. The superpositions of the corresponding loop regions, in the four domains show that the calcium binding loops in annexin I can, be divided into two classes: type II and type III. Both classes are, different from the well-known EF-hand motif (type I).

About this Structure

1AIN is a Single protein structure of sequence from Homo sapiens with CA as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of human annexin I at 2.5 A resolution., Weng X, Luecke H, Song IS, Kang DS, Kim SH, Huber R, Protein Sci. 1993 Mar;2(3):448-58. PMID:8453382

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