EF手

可用的蛋白质结构：
蛋白质家族数据库（Pfam）	结构 / ECOD
蛋白质数据库（PDB）	结构生物信息学研究合作实验室PDB; PDB欧洲; PDB日本
蛋白质数据库概述（PDBsum）	结构概述
蛋白质数据库（PDB）	1s6jA:375-402 1s6iA:375-403 1m39A:141-169 2a4jA:141-169 1oqpA:138-166 2bbnA:121-148 2bkhB:121-148 1mxeA:121-148 4cln :121-148 2bbmA:121-148 1cdmA:121-146 1lin :121-148 2bkiB:121-148 1oojA:121-148 1osa :121-148 1clm :121-147 1n0yB:121-148 1exrA:121-148 1rfjA:121-149 1ggzA:121-148 1ak8 :48-75 1sw8A:48-76 1j7oA:48-76 1f70A:48-76 1r2uA:56-84 1r6pA:56-84 1j1eA:56-84

EF手
EF手
	重组的第四双小核草履虫钙调蛋白结构
标识符
符号	efhand
蛋白质家族数据库（Pfam）	PF00036
蛋白质互联数据库（InterPro）	IPR002048
蛋白质站点（PROSITE）	PDOC00018
蛋白质结构分类数据库2（SCOP2）	1osa / SCOPe / SUPFAM
膜中蛋白质方向（OPM）蛋白质	1djx
蛋白质家族数据库（Pfam）
可用的蛋白质结构：
蛋白质家族数据库（Pfam）	结构 / ECOD
蛋白质数据库（PDB）	结构生物信息学研究合作实验室PDB; PDB欧洲; PDB日本
蛋白质数据库概述（PDBsum）	结构概述
蛋白质数据库（PDB）	1s6jA:375-402 1s6iA:375-403 1m39A:141-169 2a4jA:141-169 1oqpA:138-166 2bbnA:121-148 2bkhB:121-148 1mxeA:121-148 4cln :121-148 2bbmA:121-148 1cdmA:121-146 1lin :121-148 2bkiB:121-148 1oojA:121-148 1osa :121-148 1clm :121-147 1n0yB:121-148 1exrA:121-148 1rfjA:121-149 1ggzA:121-148 1ak8 :48-75 1sw8A:48-76 1j7oA:48-76 1f70A:48-76 1r2uA:56-84 1r6pA:56-84 1j1eA:56-84

EF手（英語：EF hand）是一种在钙结合蛋白中发现的螺旋-环-螺旋结构域或结构基序。

EF手包括一个螺旋-环-螺旋拓扑结构，就像人类的手上拇指和食指，而Ca²⁺离子与其配体就位于环内。这一结构最早在小清蛋白中发现，小清蛋白含有三个EF手结构，与钙离子结合而造成的肌肉放松有关。

EF手包含两个α螺旋，由一个短的（通常包括12个氨基酸）环状区域连接，常用于结合钙离子。EF手也出现在钙调蛋白的所有结构域和肌肉蛋白质肌钙蛋白C中。

钙离子结合位点

分类

自从EF手结构模体在1973年被描绘以来，迄今为止该家族的蛋白质已扩展到至少66个亚家族。EF手结构基元可以分为Canonical EF-hands和Pseudo EF-hands 两大类：

亚族

EPS15 homology (EH) domain – IPR000261

例子

人类基因组中，包含有EF手的蛋白质有：

ACTN1、ACTN2、ACTN3、ACTN4、APBA2BP; AYTL1; AYTL2
C14orf143; CABP1; CABP2; CABP3; CABP4; CABP5; CABP7; CALB1; CALB2; CALM2; CALM3; CALML3; CALML4; CALML5; CALML6; CALN1; CALU; CAPN1; CAPN11; CAPN2; CAPN3; CAPN9; CAPNS1; CAPNS2; CAPS; CAPS2; CAPSL; CBARA1; CETN1; CETN2; CETN3; CHP; CHP2; CIB1; CIB2; CIB3; CIB4; CRNN
DGKA; DGKB; DGKG; DST; DUOX1; DUOX2
EFCAB1; EFCAB2; EFCAB4A; EFCAB4B; EFCAB6; EFCBP1; EFCBP2; EFHA1; EFHA2; EFHB; EFHC1; EFHD1; EFHD2; EPS15; EPS15L1
FKBP10; FKBP14; FKBP7; FKBP9; FKBP9L; FREQ; FSTL1; FSTL5
GCA; GPD2; GUCA1A; GUCA1B; GUCA1C
hippocalcin; HPCAL1; HPCAL4; HZGJ
IFPS; ITSN1; ITSN2; KCNIP1; KCNIP2; KCNIP3; KCNIP4; KIAA1799
LCP1
MACF1; MRLC2; MRLC3; MST133; MYL1; MYL2; MYL5; MYL6B; MYL7; MYL9; MYLC2PL; MYLPF
NCALD; NIN; NKD1; NKD2; NLP; NOX5; NUCB1; NUCB2
OCM
PDCD6; PEF1; PKD2; PLCD1; PLCD4; PLCH1; PLCH2; PLS1; PLS3; PP1187; PPEF1; PPEF2; PPP3R1; PPP3R2; PRKCSH; PVALB
RAB11FIP3; RASEF; RASGRP; RASGRP1; RASGRP2; RASGRP3; RCN1; RCN2; RCN3; RCV1; RCVRN; REPS1; RHBDL3; RHOT1; RHOT2; RPTN; RYR2; RYR3
S100A1; S100A11; S100A12; S100A6; S100A8; S100A9; S100B; S100G; S100Z; SCAMC-2; SCGN; SCN5A; SDF4; SLC25A12; SLC25A13; SLC25A23; SLC25A24; SLC25A25; SPATA21; SPTA1; SPTAN1; SRI
TBC1D9; TBC1D9B; TCHH; TESC; TNNC1; TNNC2
USP32
VSNL1
ZZEF1

另见

锚定结构域，另一种由α-螺旋组成的钙结合结构基序。

参考文献

^ Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M. Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 A resolution. Acta Crystallogr. D Biol. Crystallogr. January 1994, 50 (Pt 1): 50–63. PMID 15299476. doi:10.1107/S0907444993007991.

延伸阅读

Branden C, Tooze J. Chapter 2: Motifs of protein structure. Introduction to Protein Structure. New York: Garland Pub. 1999: 24–25. ISBN 0-8153-2305-0.
Nakayama S, Kretsinger RH. Evolution of the EF-hand family of proteins. Annu Rev Biophys Biomol Struct. 1994, 23: 473–507. PMID 7919790. doi:10.1146/annurev.bb.23.060194.002353.
Zhou Y, Yang W, Kirberger M, Lee HW, Ayalasomayajula G, Yang JJ. Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins. Proteins. November 2006, 65 (3): 643–55. PMID 16981205. doi:10.1002/prot.21139.
Zhou Y, Frey TK, Yang JJ. Viral calciomics: interplays between Ca2+ and virus. Cell Calcium. July 2009, 46 (1): 1–17. PMID 19535138. doi:10.1016/j.ceca.2009.05.005.
Nakayama S, Moncrief ND, Kretsinger RH. Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories. J. Mol. Evol. May 1992, 34 (5): 416–48. PMID 1602495. doi:10.1007/BF00162998.
Hogue CW, MacManus JP, Banville D, Szabo AG. Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins. J. Biol. Chem. July 1992, 267 (19): 13340–7. PMID 1618836.
Bairoch A, Cox JA. EF-hand motifs in inositol phospholipid-specific phospholipase C. FEBS Lett. September 1990, 269 (2): 454–6. PMID 2401372. doi:10.1016/0014-5793(90)81214-9.
Finn BE, Forsén S. The evolving model of calmodulin structure, function and activation. Structure. January 1995, 3 (1): 7–11. PMID 7743133. doi:10.1016/S0969-2126(01)00130-7.
Stathopulos PB, Zheng L, Li GY, Plevin MJ, Ikura M. Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell. October 2008, 135 (1): 110–22. PMID 18854159. doi:10.1016/j.cell.2008.08.006.
Nelson MR, Thulin E, Fagan PA, Forsén S, Chazin WJ. The EF-hand domain: a globally cooperative structural unit. Protein Sci. February 2002, 11 (2): 198–205. PMC 2373453 . PMID 11790829. doi:10.1110/ps.33302.

外部链接

Nelson M, Chazin W. EF-Hand Calcium-Binding Proteins Data Library. Vanderbilt University. [2009-08-29]. （原始内容存档于2009-08-25）.
Haiech J. EF-hand protein database (EF-handome). European Calcium Society and the Université Libre de Bruxelles. [2009-08-29]. （原始内容存档于2009-08-09）. upon request to haiech@pharma.u-strasbg.fr
Yang J. Calciomics. Georgia State University. [2009-08-29]. （原始内容存档于2009-10-12）. prediction server for EF-hand calcium binding proteins

[pmid15299476-1] Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M. Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 A resolution. Acta Crystallogr. D Biol. Crystallogr. January 1994, 50 (Pt 1): 50–63. PMID 15299476. doi:10.1107/S0907444993007991.

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