1IRJ

Crystal Structure of the MRP14 complexed with CHAPS

Summary for 1IRJ

• Entry DOI: 10.2210/pdb1irj/pdb
• Descriptor: Migration Inhibitory Factor-Related Protein 14, CALCIUM ION, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, ... (4 entities in total)
• Functional Keywords: calgranulin b, mrp14, s100a9, ef-hand, metal binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P06702
• Total number of polymer chains: 8
• Total formula weight: 108163.35

Authors

Itou, H.,Yao, M.,Watanabe, N.,Nishihira, J.,Tanaka, I. (deposition date: 2001-10-09, release date: 2002-02-27, Last modification date: 2023-12-27)

Primary citation

Itou, H.,Yao, M.,Fujita, I.,Watanabe, N.,Suzuki, M.,Nishihira, J.,Tanaka, I.
The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent regulator protein in inflammatory process.
J.Mol.Biol., 316:265-276, 2002

PubMed Abstract: Human MRP14 (hMRP14) is a Ca(2+)-binding protein from the S100 family of proteins. This protein is co-expressed with human MRP8 (hMRP8), a homologue protein in myeloid cells, and plays an indispensable role in Ca(2+)-dependent functions during inflammation. This role includes the activation of Mac-1, the beta(2) integrin which is involved in neutrophil adhesion to endothelial cells. The crystal structure of the holo form of hMRP14 was analyzed at 2.1 A resolution. hMRP14 is distinguished from other S100 member proteins by its long C-terminal region, and its structure shows that the region is extensively flexible. In this crystal structure of hMRP14, Chaps molecules bind to the hinge region that connects two EF-hand motifs, which suggests that this region is a target-binding site of this protein. Based on a structural comparison of hMRP14 with hMRP8 and human S100A12 (hS100A12) that is another homologue protein, the character of MRP8/14 hetero-complex and the functional significance of the flexibility of the C-terminal region of hMRP14 are discussed.

PubMed: 11851337
DOI: 10.1006/jmbi.2001.5340

Experimental method

X-RAY DIFFRACTION (2.1 Å)