PDBsum entry 1ukm

Toxin

PDB id

1ukm

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Contents

			Protein chains

					131 a.a. *


					124 a.a. *

			Ligands

					GOL ×4


					NAG

			Metals

					_CL

			Waters ×250

* Residue conservation analysis

PDB id:

1ukm

Links

Name:

Toxin

Title:

Crystal structure of ems16, an antagonist of collagen receptor integrin alpha2beta1 (gpia/iia)

Structure:

Ems16 a chain. Chain: a. Fragment: residues 1-134. Synonym: ems16 subunit a. Ems16 b chain. Chain: b. Fragment: residues 1-128. Synonym: ems16 subunit b

Source:

Echis multisquamatus. Organism_taxid: 93050. Secretion: venom. Secretion: venom

Biol. unit:

Dimer (from PQS)

Resolution:

1.90Å

R-factor:

0.196

R-free:

0.233

Authors:

K.Horii,D.Okuda,T.Morita,H.Mizuno

Key ref:

K.Horii et al. (2003). Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus. Biochemistry, 42, 12497-12502. PubMed id: 14580195 DOI: 10.1021/bi034890h

Date:

27-Aug-03

Release date:

04-Nov-03

PROCHECK

	Headers

	References

Protein chain

Q7T2Q1 (SLA_ECHML) - Snaclec EMS16 subunit alpha from Echis multisquamatus

Seq: Struc:					157 a.a. 131 a.a.

Protein chain

Q7T2Q0 (SLB_ECHML) - Snaclec EMS16 subunit beta from Echis multisquamatus

Seq: Struc:					154 a.a. 124 a.a.*

Key:

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1021/bi034890h	Biochemistry 42:12497-12502 (2003)
PubMed id: 14580195

Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus.
K.Horii, D.Okuda, T.Morita, H.Mizuno.

ABSTRACT

Snake venoms contain a number of hemostatically active C-type lectin-like proteins (CLPs), which affect the blood coagulation system, endothelial cells, and platelets. CLPs have broad similarities in structure and possess distinct biological functions. EMS16, a CLP from Echis multisquamatus venom, which is a potent and selective inhibitor of the collagen receptor, glycoprotein Ia/IIa (integrin alpha2beta1), has been used in the present study to examine structure-function relationships in venom CLPs by X-ray crystallography. The structure of EMS16, determined at a resolution of 1.9 A, revealed a heterodimer involved with domain swapping of the central loop as observed in the structures of other CLPs. A part of the glycan was observed and identified as N-acetyl-D-glucosamine (GlcNAc) in the electron density map at Asn21 of subunit B, an expected glycosylation site. EMS16 had a unique, positively charged electrostatic potential patch on the concave surface that may qualify as a site for interaction with the I-domain of the glycoprotein Ia/IIa.

Literature references that cite this PDB file's key reference

PubMed id

Reference

15639110

H.L.Messmore, W.P.Jeske, W.Wehrmacher, E.Coyne, S.Mobarhan, L.Cho, F.S.Leya, and J.F.Moran (2005).
Antiplatelet agents: current drugs and future trends.

Hematol Oncol Clin North Am, 19, 87.

15502319

G.Xu, M.Teng, L.Niu, P.Liu, Y.Dong, Q.Liu, Q.Huang, and Q.Hao (2004).
Purification, characterization, crystallization and preliminary X-ray crystallographic analysis of two novel C-type lectin-like proteins: Aall-A and Aall-B from Deinagkistrodon acutus venom.

Acta Crystallogr D Biol Crystallogr, 60, 2035-2037.

15388950

Y.L.Wang, K.X.Goh, W.G.Wu, and C.J.Chen (2004).
Purification, crystallization and preliminary X-ray crystallographic analysis of a cysteine-rich secretory protein (CRISP) from Naja atra venom.

Acta Crystallogr D Biol Crystallogr, 60, 1912-1915.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.